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Peptide bond formation | Macromolecules | Biology | Khan Academy
 
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How amino acids (including ones in zwitterion form) form peptide bonds (peptide linkages) through a condensation reaction (dehydration synthesis). Watch the next lesson: https://www.khanacademy.org/science/biology/macromolecules/proteins-and-amino-acids/v/overview-of-protein-structure?utm_source=YT&utm_medium=Desc&utm_campaign=biology Missed the previous lesson? https://www.khanacademy.org/science/biology/macromolecules/proteins-and-amino-acids/v/introduction-to-amino-acids?utm_source=YT&utm_medium=Desc&utm_campaign=biology Biology on Khan Academy: Life is beautiful! From atoms to cells, from genes to proteins, from populations to ecosystems, biology is the study of the fascinating and intricate systems that make life possible. Dive in to learn more about the many branches of biology and why they are exciting and important. Covers topics seen in a high school or first-year college biology course. About Khan Academy: Khan Academy offers practice exercises, instructional videos, and a personalized learning dashboard that empower learners to study at their own pace in and outside of the classroom. We tackle math, science, computer programming, history, art history, economics, and more. Our math missions guide learners from kindergarten to calculus using state-of-the-art, adaptive technology that identifies strengths and learning gaps. We've also partnered with institutions like NASA, The Museum of Modern Art, The California Academy of Sciences, and MIT to offer specialized content. For free. For everyone. Forever. #YouCanLearnAnything Subscribe to Khan Academy's Biology channel: https://www.youtube.com/channel/UC82qE46vcTn7lP4tK_RHhdg?sub_confirmation=1 Subscribe to Khan Academy: https://www.youtube.com/subscription_center?add_user=khanacademy
Views: 234679 Khan Academy
Amino Acid Peptide Linkage and Hydrolysis Reactions
 
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http://leah4sci.com/aminoacids Presents: Amino Acid Peptide Linkage and Hydrolysis Tired of conflicting and confusing MCAT advice? Grab My FREE guide for everything MCAT prep: http://mcatstrategyguide.com/guide In this video you'll see a step by step explanation of peptide linkage, how amino acids are connected, to make polypeptides and ultimately proteins. Then you'll see hydrolysis at the atomic level to show how to get back to individual peptides once again. Links & Resources Mentioned In This Video: Functional Group Cheat Sheet: http://leah4sci.com/functional-group-priority-cheat-sheet/ Full MCAT Video List: http://leah4sci.com/MCAT Catch the entire Amino Acids Video Series, along with my amino acid cheat sheet, tutorials, and practice quiz on my website at http://leah4sci.com/aminoacids Need more help? I offer private online MCAT tutoring. Details http://leah4sci.com/mcat-tutoring/ Finally, for questions and comments, find me on social media here: Facebook: https://www.facebook.com/Leah4Sci Twitter: https://twitter.com/Leah4Sci Instagram: https://www.instagram.com/leah4sci/ Google+ : https://plus.google.com/u/0/+LeahFisch Pinterest: http://www.pinterest.com/leah4sci/
Views: 11525 Leah4sciMCAT
Peptide bond structure | formation and rotation of peptide bonds
 
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This peptide bond structure lecture explains the peptide bond formation and rotation of angles. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching In this video, the structure and formation of peptide bonds is illustrated. A peptide bond (amide bond) is a covalent chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, causing the release of a molecule of water (H2O), hence the process is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids. The resulting C(O)NH bond is called a peptide bond, and the resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called a peptide link. Polypeptides and proteins are chains of amino acids held together by peptide bonds, as is the backbone of PNA. A peptide bond can be broken by hydrolysis (the adding of water). In the presence of water they will break down and release 8--16 kilojoule/mol (2--4 kcal/mol) [1] of free energy. This process is extremely slow (up to 1000 years). In living organisms, the process is facilitated by enzymes. Living organisms also employ enzymes to form peptide bonds; this process requires free energy. The wavelength of absorbance for a peptide bond is 190--230 nm[2] (which makes it particularly susceptible to UV radiation). Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page Biochemistry, 4th Edition Donald Voet, Judith G. Voet November 2010, ©2011
Views: 16741 Shomu's Biology
1 How Amino Acids Form Protein
 
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How Amino Acids Form Protein
Views: 53161 Random Videos
Peptide Bonds
 
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Views: 74126 360Edmlaurence
Peptide bonds: Formation and cleavage | Chemical processes | MCAT | Khan Academy
 
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Peptide bonds are formed when the amine group of one amino acid binds with the carbonyl carbon of another amino acid. We will learn more about peptide bonds and how the cleaving process occurs. By Tracy Kovach. Created by Tracy Kim Kovach. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/chemical-processes/amino-acids-peptides-proteins-5d/v/special-cases-histidine-proline-glycine-cysteine?utm_source=YT&utm_medium=Desc&utm_campaign=mcat Missed the previous lesson? https://www.khanacademy.org/test-prep/mcat/chemical-processes/amino-acids-peptides-proteins-5d/v/central-dogma-revisited?utm_source=YT&utm_medium=Desc&utm_campaign=mcat MCAT on Khan Academy: Go ahead and practice some passage-based questions! About Khan Academy: Khan Academy offers practice exercises, instructional videos, and a personalized learning dashboard that empower learners to study at their own pace in and outside of the classroom. We tackle math, science, computer programming, history, art history, economics, and more. Our math missions guide learners from kindergarten to calculus using state-of-the-art, adaptive technology that identifies strengths and learning gaps. We've also partnered with institutions like NASA, The Museum of Modern Art, The California Academy of Sciences, and MIT to offer specialized content. For free. For everyone. Forever. #YouCanLearnAnything Subscribe to Khan Academy’s MCAT channel: https://www.youtube.com/channel/UCDkK5wqSuwDlJ3_nl3rgdiQ?sub_confirmation=1 Subscribe to Khan Academy: https://www.youtube.com/subscription_center?add_user=khanacademy
Views: 264957 khanacademymedicine
Protein - Structure Of Protein - What Is Protein Made Of - Structure Of Amino Acids Building Blocks
 
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In this video we discuss the structure of protein and the structure of amino acids. We cover how amino acids link together to form proteins. Transcript/notes Protein structure All Proteins contain 4 elements, carbon, hydrogen, oxygen and nitrogen, however, some proteins contain phosphorus, sulfur, iron, zinc, magnesium and other trace metals. Proteins are giant macro molecules that are made up of amino acid building blocks. Amino acids can link together to form long chains, typically a protein consists of 100 or more amino acids linked together. There are 20 different standard amino acids that your body requires for healthy function. These amino acids are often classified as essential and non-essential amino acids. Nonessential amino acids are amino acids that our bodies can produce even if we don’t get them from the food we eat. There are 11 non-essential amino acids (list). Essential amino acids cannot be made by the body, so, they must come from foods we eat. There are 9 essential amino acids. The basic structure of amino acids is that they consist of a alpha carbon, a carboxyl group, which is a carbon, oxygen, hydrogen, hydrogen group, a lone hydrogen atom, an amino group, which is a nitrogen, hydrogen, hydrogen group, and a side chain or functional group, which is often referred to as an R-group. The formation of the side chain is what makes amino acids different from one another. On the screen is the structural formulas for all 20 of the standard amino acids along with the amino acid selenocysteine, as some sources list it as a 21st standard amino acid. As you can see, they all have the same chemical backbone, and the only difference is their unique functional R group. These functional R groups of have chemical characteristics that allow amino acids to be organized into groups. Here we have the non polar amino acids, non polar meaning the electrons are shared equally in the molecule, these are hydrophobic, so they tend to be repelled from water. Here are the polar amino acids; these molecules can have interactions with other polar amino acids and with water molecules. Here are the charged amino acids, since they are charged, an ionic bond can form between an R group with a negative charge and an R group with a positive charge. And here are some amino acids that are considered to have unique structures. As was stated earlier, amino acids can link together to form long chains, there is an almost infinite number of different variations of chains that can be formed from amino acids. Each chain can have different characteristics with different chemical properties. When 2 amino acids join together they form what is called a peptide bond. A peptide bond is when the carboxyl or carbon, oxygen, hydrogen, hydrogen group of one amino acid bonds with the amino nitrogen, hydrogen, hydrogen group of another amino acid, as you can see here (on screen). This is done through a dehydration synthesis reaction, as the amino group involved in the bond loses a hydrogen atom, and the carboxyl group involved in the bond loses an oxygen and hydrogen. So, the peptide bonding results in the release of a water h2o molecule. More amino acids can link in, again releasing water molecules, and form what is called a polypeptide chain. As you can see in this polypeptide chain, at one end, an amino group remains, called the N terminal, and at the other end a carboxyl group remains, the C terminal. Typically a protein consists of 100 or more amino acids linked together. Some proteins are single polypeptide chains, and other proteins have polypeptide chains linked together. Individual amino acids can also be released from a peptide chain, by the decomposition reaction hydrolysis. In hydrolysis, a water molecule is added, breaking the peptide bond and freeing up amino acids. So, amino acids link together in a variety of sequences to form different types of proteins. Some of these proteins serve as enzymes, which help speed up metabolic reactions in the body, some serve as hormones and help regulate certain functions in the body, some proteins help form the structure of various tissues in the body, these are just a few of the many, many functions that proteins have in the body.
Views: 11608 Whats Up Dude
Origin: Probability of a Single Protein Forming by Chance
 
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Mathematical Basis for Probability Calculations Used in (the film) Origin Excerpt: Putting the probabilities together means adding the exponents. The probability of getting a properly folded chain of one-handed amino acids, joined by peptide bonds, is one chance in 10^74+45+45, or one in 10^164 (Meyer, p. 212). This means that, on average, you would need to construct 10^164 chains of amino acids 150 units long to expect to find one that is useful. http://www.originthefilm.com/mathematics.php Minimal Complexity Relegates Life Origin Models To Fanciful Speculation - Nov. 2009 Excerpt: Based on the structural requirements of enzyme activity Axe emphatically argued against a global-ascent model of the function landscape in which incremental improvements of an arbitrary starting sequence "lead to a globally optimal final sequence with reasonably high probability". For a protein made from scratch in a prebiotic soup, the odds of finding such globally optimal solutions are infinitesimally small- somewhere between 1 in 10exp140 and 1 in 10exp164 for a 150 amino acid long sequence if we factor in the probabilities of forming peptide bonds and of incorporating only left handed amino acids. http://www.arn.org/blogs/index.php/2/2009/11/10/minimal_complexity_relegates_life_origin The Case Against a Darwinian Origin of Protein Folds - Douglas Axe - 2010 Excerpt Pg. 11: "Based on analysis of the genomes of 447 bacterial species, the projected number of different domain structures per species averages 991. Comparing this to the number of pathways by which metabolic processes are carried out, which is around 263 for E. coli, provides a rough figure of three or four new domain folds being needed, on average, for every new metabolic pathway. In order to accomplish this successfully, an evolutionary search would need to be capable of locating sequences that amount to anything from one in 10^159 to one in 10^308 possibilities, something the neo-Darwinian model falls short of by a very wide margin." http://bio-complexity.org/ojs/index.php/main/article/view/BIO-C.2010.1 “We have no idea how the molecules that compose living systems could have been devised such that they would work in concert to fulfill biology’s functions. We have no idea how the basic set of molecules, carbohydrates, nucleic acids, lipids, and proteins, were made and how they could have coupled into the proper sequences, and then transformed into the ordered assemblies until there was the construction of a complex biological system, and eventually to that first cell. Nobody has any idea how this was done when using our commonly understood mechanisms of chemical science. Those that say they understand are generally wholly uninformed regarding chemical synthesis. Those that say “Oh, this is well worked out,” they know nothing, nothing about chemical synthesis – Nothing! Further cluelessness – From a synthetic chemical perspective, neither I nor any of my colleagues can fathom a prebiotic molecular route to construction of a complex system. We cannot figure out the prebiotic routes to the basic building blocks of life: carbohydrates, nucleic acids, lipids, and proteins. Chemists are collectively bewildered. Hence I say that no chemist understands prebiotic synthesis of the requisite building blocks let alone their assembly into a complex system. That’s how clueless we are. I’ve asked all of my colleagues – National Academy members, Nobel Prize winners -I sit with them in offices; nobody understands this. So if your professors say it’s all worked out, your teachers say it’s all worked out, they don’t know what they’re talking about. It is not worked out. You cannot just refer this to somebody else; they don’t know what they’re talking about.” - James Tour – one of the top ten leading chemists in the world The Origin of Life: An Inside Story - March 2016 Lecture with James Tour https://www.youtube.com/watch?v=_zQXgJ-dXM4
Views: 350884 Philip C
How to Connect Amino Acids to Make a Polypeptide
 
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In this video I talk about how amino acids are bonded together thru a peptide bond.
Views: 1037 Mr Biology360
Ionic and Covalent Bonds, Hydrogen Bonds, van der Waals - 4 types of Chemical Bonds in Biology
 
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There are four types of chemical bonds essential for life to exist: Ionic Bonds, Covalent Bonds, Hydrogen Bonds, and van der Waals interactions. We need all of these different kinds of bonds to play various roles in biochemical interactions. These bonds vary in their strengths. In Chemistry, we think of Ionic Bonds and Covalent bonds as having an overlapping range of strengths. But remember, in biochemistry, everything is happening in the context of water. This means Ionic bonds tend to dissociate in water. Thus, we will think of these bonds in the following order (strongest to weakest): Covalent, Ionic, Hydrogen, and van der Waals. Also note that in Chemistry, the weakest bonds are more commonly referred to as “dispersion forces.” Related Chemistry video: Ionic Bonds vs Covalent Bonds http://bit.ly/2cUG6C8 Our series on Biology is aimed at the first-year college level, including pre-med students. These videos should also be helpful for students in challenging high school biology courses. Perfect for preparing for the AP Biology exam or the Biology SAT. Also appropriate for advanced homeschoolers. You can also follow along if you are just curious, and would like to know more about this fascinating subject. ***** Our current biology textbook recommendation is Campbell Biology from Pearson. 10th edition Amazon Link: http://amzn.to/2mahQTi 11th edition Amazon Link: http://amzn.to/2m7xU6w Amazon Used Textbooks - Save up to 90% http://amzn.to/2pllk4B For lighter reading, we recommend: I Contain Multitudes: The Microbes Within Us and a Grander View of Life by Ed Yong http://amzn.to/2pLOddQ Lab Girl by Hope Jahren http://amzn.to/2oMolPg ***** This video was made possible by the generous donations of our Patrons on Patreon. We dedicate this video to our VIP Patron, Vishal Shah. We’re so thankful for your support! ***** Please Subscribe so you'll hear about our newest videos! http://bit.ly/1ixuu9W If you found this video helpful, please give it a "thumbs up" and share it with your friends! If you'd like to support more great educational videos from Socratica, please consider becoming our Patron on Patreon! https://www.patreon.com/socratica ***** Written and Produced by Kimberly Hatch Harrison About our instructor: Kimberly Hatch Harrison received degrees in Biology and English Literature from Caltech before working in pharmaceuticals research, developing drugs for autoimmune disorders. She then continued her studies in Molecular Biology (focusing on Immunology and Neurobiology) at Princeton University, where she began teaching as a graduate student. Her success in teaching convinced her to leave the glamorous world of biology research and turn to teaching full-time, accepting a position at an exclusive prep school, where she taught biology and chemistry for eight years. She is now the head writer and producer of Socratica Studios. ****** Creative Commons Picture Credits: Salt crystals https://en.wikipedia.org/wiki/File:Halit-Kristalle.jpg Author: W.J. Pilsak Hydrogen Bonding in water https://en.wikipedia.org/wiki/File:3D_model_hydrogen_bonds_in_water.svg Author: Qwerter Products in this video: Preparing for the Biology AP* Exam (School Edition) (Pearson Education Test Prep) - http://amzn.to/2qJVbxm Cracking the AP Biology Exam, 2017 Edition: Proven Techniques to Help You Score a 5 (College Test Preparation) - http://amzn.to/2qB3NsZ Cracking the SAT Biology E/M Subject Test, 15th Edition (College Test Preparation) - http://amzn.to/2qJIfHN
Views: 44567 Socratica
Atomic Hook-Ups - Types of Chemical Bonds: Crash Course Chemistry #22
 
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Atoms are a lot like us - we call their relationships "bonds," and there are many different types. Each kind of atomic relationship requires a different type of energy, but they all do best when they settle into the lowest stress situation possible. The nature of the bond between atoms is related to the distance between them and, like people, it also depends on how positive or negative they are. Unlike with human relationships, we can analyze exactly what makes chemical relationships work, and that's what this episode is all about. If you are paying attention, you will learn that chemical bonds form in order to minimize the energy difference between two atoms or ions; that those chemical bonds may be covalent if atoms share electrons, and that covalent bonds can share those electrons evenly or unevenly; that bonds can also be ionic if the electrons are transferred instead of shared: and how to calculate the energy transferred in an ionic bond using Coulomb's Law. -- Table of Contents Bonds Minimize Energy 01:38 Covalent Bonds 03:18 Ionic Bonds 05:37 Coulomb's Law 05:51 -- Want to find Crash Course elsewhere on the internet? Facebook - http://www.facebook.com/YouTubeCrashCourse Twitter - http://www.twitter.com/TheCrashCourse Tumblr - http://thecrashcourse.tumblr.com Support CrashCourse on Subbable: http://subbable.com/crashcourse
Views: 1808935 CrashCourse
Protein Shape - Levels Of Protein Structure - Shape Of Proteins - What Is Protein Denaturation
 
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In this video we discuss the 4 different levels of protein shape, as we cover primary, secondary, tertiary or the third level, and quaternary or the fourth level. We also discuss the denaturation of protein and some things that cause it. Protein shape There are 4 different levels of protein structure, or protein shape. Primary, secondary, tertiary or the third level, and quaternary or the fourth level. The primary or 1st level of protein structure is a chain like or linear sequence of amino acids joined by peptide bonds as you see here. The secondary or 2nd level has 2 shapes, an alpha helix or coil like formation, or folded pattern called a beta sheet. In both of these structures hydrogen bonds between the R groups of the amino acids stabilize the shape of the protein. The tertiary or 3rd level of protein structure involves more folding and bonding of the secondary structure. The coils may even touch each other as some covalent bonds form from the sharing of electrons between different amino acids, but most of these twists and folds occur from the result of ionic bonds between positively and negatively charged r groups of amino acids. The quaternary or 4th level is where clusters of more than one polypeptide chain link together to form a giant molecule. Many different types of bonds may be formed within this structure. The shape of a protein is important, for instance, fibrous proteins are extended linear proteins that are part of ligaments, tendons and muscles, and globular proteins fold into almost spherical shapes and have their hydrophobic or water fearing r groups buried deep within the core, and their hydrophilic or water loving r groups extended out into the water when in an aqueous environment. Proteins take their shape based on the job they are required to perform and some have moving parts that are important to their functions. Proteins can have their structure or shaped by denaturation. When this happens, the protein is no longer able to carry out its job. Denaturation can take place because of change of temperature, change in pH, or in the presence of certain hazardous chemicals.
Views: 15903 Whats Up Dude
Ramachandran plot
 
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This tutorial about the Ramachandran plot explanation for protein secondary structures. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching This video explains the importance of Ramachandran plot to study protein chemistry. A Ramachandran plot (also known as a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan,[1] is a way to visualize backbone dihedral angles ψ against φ of amino acid residues in protein structure. The figure at left illustrates the definition of the φ and ψ backbone dihedral angles[2] (called φ and φ' by Ramachandran). The ω angle at the peptide bond is normally 180°, since the partial-double-bond character keeps the peptide planar.[3] The figure at top right shows the allowed φ,ψ backbone conformational regions from the Ramachandran et al. 1963 and 1968 hard-sphere calculations: full radius in solid outline, reduced radius in dashed, and relaxed tau (N-Calpha-C) angle in dotted lines.[4] Because dihedral angle values are circular and 0° is the same as 360°, the edges of the Ramachandran plot "wrap" right-to-left and bottom-to-top. For instance, the small strip of allowed values along the lower-left edge of the plot are a continuation of the large, extended-chain Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page Biochemistry, 4th Edition Donald Voet, Judith G. Voet November 2010, ©2011
Views: 116109 Shomu's Biology
Amino Acids - What are Amino Acids - What Do Amino Acids Do
 
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In this video I discuss what are amino acids, what are amino acids made of, and what do amino acids do in the body. I also cover what are peptide bonds, polypeptide chains, how amino acids form proteins, some functions of amino acids, and what are amino acids used to build. Transcript We are going to start by looking at the molecular structure of a typical amino acid, don’t worry, I am going to make it easy to understand. The basic structure of amino acids is that they consist of a carboxyl group, a lone hydrogen atom, an amino group, and a side chain, which is often referred to as an R-group. The formation of the side chain is what makes amino acids different from one another. As you can see in this diagram, these 4 are all connected to a carbon atom, which is referred to as the alpha carbon. Not every amino acid follows this exact structure, but, most do. On the screen I have 3 different amino acids, lysine, tryptophan, and leucine. You can see that each has a carboxyl group, an alpha carbon, a amino group, and an R-group that is different from each other. There are 23 total amino acids that are proteinogenic. Proteinogenic amino acids are precursors to proteins, which means they are compounds that participate in a chemical reaction to produce another compound. Of these 23 amino acids, 20 of them are called standard amino acids, and the other 3 are non-standard amino acids. These are listed on the screen. In this video we are going to focus on the standard amino acids, as they are what make up proteins. These amino acids can be classified many different ways, we are going to classify them in a basic nutritional way. Essential and nonessential. Essential amino acids cannot be made by the body, so, they must come from foods we eat. Nonessential amino acids are amino acids that our bodies can produce even if we don’t get them from the food we eat. There is a subgroup of nonessential amino acids that are considered to be conditional amino acids. The list of conditional amino acids is not definitive. For instance, in times of illness or stress, there are certain amino acids the body cant produce sufficiently, and children's bodys haven’t developed the ability to produce certain amino acids yet. There are 9 essential and 11 nonessential amino acids, ive listed them on the screen. So, how do amino acids form proteins? Proteins are built from the 20 standard amino acids. Well, the first thing that happens is that 2 amino acids come together to form a peptide bond. A peptide bond is when the carboxyl group of one amino acid bonds with the amino group of another amino acid, as you can see here. If you notice 2 hydrogen atoms and one oxygen atom have been removed from the peptide bonding process. So, the peptide bonding results in the release of a water molecule…h20. But, we are not finished. More amino acids can link in, and form what is called a polypeptide chain. Some proteins are single polypeptide chains, and other proteins have polypeptide chains linked together. Not all protein contains all 20 of the standard amino acids. Not all protein contains all 20 of the standard amino acids. Proteins are often labeled as complete or incomplete protein. A Complete protein is a protein source that contains a sufficient quantity of all 9 of the essential amino acids that we discussed earlier. An incomplete protein does not contain a sufficient quantity of all 9 of the essential amino acids. Complete protein foods include…animal foods such as red meat, poultry, pork and fish. Eggs and dairy products such as cows milk, yogurt, and cheese. Plant foods such as soy products, black beans, kidney beans, pumpkin seeds, quinoa, pistachios, just to name a few. You can also combine incomplete protein foods to create a complete protein meal. Amino acids also make up most enzymes. These Enzymes are proteins, so they are made by linking amino acids together in a specific and unique order. This chain of amino acids then forms a unique shape that allows the enzyme created to serve a single specific purpose. Enzymes function as catalysts, which means that they speed up the rate at which metabolic processed and reactions occur. Amino acids can also be metabolized for energy. Some hormones like epinephrine, also known as adrenaline, are amino acid derived. Some neurotransmitters like serotonin are derived from amino acids. The amino acid arginine is a precursor of nitric oxide, which helps regulate blood pressure, improves sleep quality and increases endurance and strength. Glutathione, which is a powerful antioxidant is formed from amino acids. Other sources... https://en.wikipedia.org/wiki/Amino_acid http://www.fitday.com/fitness-articles/nutrition/proteins/incomplete-vs-complete-proteins.html http://www.ivyroses.com/HumanBiology/Nutrition/Amino_Acids.php
Views: 55969 Whats Up Dude
Torsional angle
 
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This protein structure lecture explains about the torsional angle in amino acid structure. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching This video tutorial explains about the torsional angles and their applications in protein chemistry. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page Biochemistry, 4th Edition Donald Voet, Judith G. Voet November 2010, ©2011
Views: 50199 Shomu's Biology
B.2 Amino acids - structure and bonding (SL)
 
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Understandings: Proteins are polymers of 2-amino acids, joined by amide links (also known as peptide bonds).
Views: 4256 Mike Sugiyama Jones
Amino Acids 4. Formation of a Dipeptide.
 
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This video looks at the formation of a dipeptide in a condensation reaction. It shows the two possible dipeptides that can be formed from glycine and alanine. This is one in a series of videos looking at the chemistry of amino acids and proteins. Other in the series look at: the structures of amino acids; the zwitterion and its amphoteric properties; the reactions of the amino acid glycine (2-aminoethanoic acid) with sodium hydroxide, sodium carbonate and aqueous copper (II) sulfate solution; formation of the backbone structure of a polypeptide; a general account of secondary structure; the alpha helix secondary structure; the beta-pleated sheet secondary structure; fibrous proteins verses globular proteins; protein hydrolysis
Views: 10766 FranklyChemistry
Amino Acids
 
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It's time to start learning about all the monomers that make up large biomolecules, and the first one we will look at is the amino acid. These make up proteins, which is most of what you are, so this is pretty important stuff! To support this channel and keep up on STEM news at the same time, click on the link below and subscribe to this FREE newsletter: http://www.jdoqocy.com/click-9021241-13591026 Subscribe: http://bit.ly/ProfDaveSubscribe [email protected] http://patreon.com/ProfessorDaveExplains http://professordaveexplains.com http://facebook.com/ProfessorDaveExpl... http://twitter.com/DaveExplains General Chemistry Tutorials: http://bit.ly/ProfDaveGenChem Organic Chemistry Tutorials: http://bit.ly/ProfDaveOrgChem Biochemistry Tutorials: http://bit.ly/ProfDaveBiochem Classical Physics Tutorials: http://bit.ly/ProfDavePhysics1 Modern Physics Tutorials: http://bit.ly/ProfDavePhysics2 Mathematics Tutorials: http://bit.ly/ProfDaveMaths Biology Tutorials: http://bit.ly/ProfDaveBio American History Tutorials: http://bit.ly/ProfDaveAmericanHistory
Views: 238368 Professor Dave Explains
Proteins
 
09:16
Paul Andersen explains the structure and importance of proteins. He describes how proteins are created from amino acids connected by dehydration synthesis. He shows the importance of chemical properties in the R-groups of individual amino acids in the polypeptide. He explains the four levels of protein folding and gives you an opportunity to fold proteins of your own using the game Foldit: Download the video game foldit here: http://fold.it/portal/ Intro Music Atribution Title: I4dsong_loop_main.wav Artist: CosmicD Link to sound: http://www.freesound.org/people/CosmicD/sounds/72556/ Creative Commons Atribution License
Views: 947717 Bozeman Science
Amino Acids 5. Formation of a Polypeptide.
 
03:08
This video looks at the formation of a polypeptide in a condensation reaction. It uses animation to show amino acids reacting together to form a long chain polymer molecule. This is one in a series of videos looking at the chemistry of amino acids and proteins. Other in the series look at: the structures of amino acids; the zwitterion and its amphoteric properties; the reactions of the amino acid glycine (2-aminoethanoic acid) with sodium hydroxide, sodium carbonate and aqueous copper (II) sulfate solution; formation of two possible dipeptides by the condensation reactions of glycine and alanine; a general account of secondary structure; the alpha helix secondary structure; the beta-pleated sheet secondary structure; fibrous proteins verses globular proteins; protein hydrolysis
Views: 4500 FranklyChemistry
The Peptide Bond: Formation and Cleavage
 
07:11
How is the peptide bond formed and how can it be cleaved?
Views: 29928 khanacademymedicine
Covalent Bonding | #aumsum
 
06:11
Covalent Bonding. Noble gases have complete outer electron shells, which make them stable. The coming together and sharing of electron pairs leads to the formation of a chemical bond known as a covalent bond. Two chlorine atoms come together and share their electrons to form a molecule of chlorine. In this way, each atom will have eight electrons in its valence shell. As a single pair of electrons is shared between them, the bond is known as a single covalent bond. A single covalent bond is represented by a single dash between the atoms. When two oxygen atoms come together, they each share 2 electrons to complete their octets. Since they share two pairs of electrons, there is a double bond between the oxygen atoms. Similarly, Nitrogen atoms share a triple covalent bond to form a molecule of Nitrogen.
Views: 1452295 It's AumSum Time
Drawing Peptides
 
07:11
This video discusses how to draw a peptide using a strategy that ensures the backbone is drawn correctly.
Views: 275 Dr. G
Protein Structure
 
10:50
Everyone has heard of proteins. What are they on the molecular level? They're polymers of amino acids, of course. They make up most of your body, so we have to understand their structure very well! Check this out to learn the hierarchy of protein structure so that we can later learn all about what different types of proteins can do. To support this channel and keep up on STEM news at the same time, click on the link below and subscribe to this FREE newsletter: http://www.jdoqocy.com/click-9021241-13591026 Subscribe: http://bit.ly/ProfDaveSubscribe [email protected] http://patreon.com/ProfessorDaveExplains http://professordaveexplains.com http://facebook.com/ProfessorDaveExpl... http://twitter.com/DaveExplains General Chemistry Tutorials: http://bit.ly/ProfDaveGenChem Organic Chemistry Tutorials: http://bit.ly/ProfDaveOrgChem Biochemistry Tutorials: http://bit.ly/ProfDaveBiochem Classical Physics Tutorials: http://bit.ly/ProfDavePhysics1 Modern Physics Tutorials: http://bit.ly/ProfDavePhysics2 Mathematics Tutorials: http://bit.ly/ProfDaveMaths Biology Tutorials: http://bit.ly/ProfDaveBio American History Tutorials: http://bit.ly/ProfDaveAmericanHistory
Views: 326029 Professor Dave Explains
#04 Biochemistry Protein Primary/Secondary Structure Lecture for Kevin Ahern's BB 450/550
 
48:58
1. Contact me at [email protected] / Friend me on Facebook (kevin.g.ahern) 2. Download my free biochemistry book at http://www.davincipress.com/freeforall.html 3. Take my free iTunes U course at https://itunes.apple.com/us/course/biochemistry/id556410409 4. Lecturio videos for medical students - https://www.lecturio.com/medical-courses/biochemistry.course 5. Course video channel at http://www.youtube.com/user/oharow/videos?view=1 6. Check out all of my free workshops at http://oregonstate.edu/dept/biochem/ahern/123.html 7. Check out my Metabolic Melodies at http://www.davincipress.com/ 8. My courses can be taken for credit (wherever you live) via OSU's ecampus. For details, see http://ecampus.oregonstate.edu/soc/ecatalog/ecourselist.htm?termcode=all&subject=BB 9. Course materials at http://davincipress.com/bb450.html Protein Structure II 1.The sequence of amino acids in a protein is ultimately responsible for all of the properties a protein has. The sequence of amino acids of a protein is referred to as its primary structure. 2. Peptide bonds form resonance structures such that the bond itself behaves like a double bond. Double bonds cannot rotate (unlike single bonds) and thus they define a plane. Alpha carbons on either side of a peptide bond are generally arranged in a trans configuration (about 10,000 trans to one cis), except when proline is involved. Peptide bonds involving proline favor the trans by about a 100 to 1 ratio. 3. The bonds around the alpha carbon (the carbon bonded to both an amino group and a carboxy group) can both rotate, however, because they are single bonds. One can thus describe a polypeptide as a series of planes separated by an alpha carbon, with the planes each being rotated a certain number of degrees relative to the alpha carbon. If we think of the alpha carbon as being in between two planes, then the plane on the left can rotate (theoretically) 360 degrees and the plane on the right can also theoretically rotate 360 degrees. These angles of rotation of planes are referred to as phi and psi angles. Phi refers to the rotational angle around the single bond between the alpha amino group and the alpha carbon. Psi refers to the rotational angle around the single bond between the alpha carbon and the alpha carboxyl group. 4. Ramachandran, recognized that not all rotations of phi and psi would be theoretically feasible because steric hindrance would preclude some rotational positions. He plotted theoretical rotations of psi versus phi and calculated which of these angles would provide stable structures. The regions of stability turn out to be regions of known stability from protein structures that have been determined. 5. The secondary structure of a polypeptide refers to regular/repeating structure(s) arising from interactions between amino acids that are relatively close together in primary sequence. This means less than 10 amino acids away. 6. One protein secondary structure that is stable in both real proteins and theoretical ones (Ramachandran plots) is the alpha helix. Alpha helices are one type of secondary structure and form coils. 7. Hydrogen bonds are primary forces stabilizing secondary structures. In alpha helices, carbonyl oxygen from a peptide bond forms a hydrogen bond with an amine nitrogen of another peptide bond four amino acids distant. 8. Certain amino acids with simple side chains, such as alanine, are very favorable for formation of alpha helices, whereas bulky (tryptophan) or cyclic (proline) amino acids tend to disrupt alpha helices. . 9. Another type of common secondary structure commonly found in protein is the beta strand (note that the term beta sheet refers to layering together of beta strands together), which consists of amino acid backbones in a V shape (like the pleats of a drape). A beta strand can be thought of as a helix in two dimensions. 10. Beta sheets arise from arrangement of beta strands. These arise from interactions (hydrogen bonds) between beta strands (parallel or antiparallel), such that the carbonyl oxygen of one side interacts with the amine hydrogen with the other. 11. Essential features of proteins that are essential for their overall structure are turns. Turns interrupt secondary structure (alpha helices and beta strands) and often involve proline and glycine residues. 12. Another type of fibrous protein is collagen, the most abundant protein in your body. It contains three intertwined helices comprised of abundant repeating units of glycine, proline, and hydroxylproline 13. Hydroxylation of proline is a post-translational modification (occurs after the protein is made) and the hydroxyls are placed there in a reaction that uses vitamin C. 14. The hydroxyls of hydroxyproline can react with other, forming covalent cross-links that make the collagen fibers more sturdy.
Views: 55521 Kevin Ahern
Dehydration Synthesis And Hydrolysis - What Is Anabolism - What Is Catabolism
 
02:47
In this video we discuss the processes of hydrolysis and dehydration synthesis, and how these both use water. We also discuss how they are either catabolism or anabolism. Hydrolysis and dehydration synthesis Metabolism, or body chemistry is often used to generally describe all of the chemical reactions that occur in body cells. The two major types of metabolic activity that occur in the body are catabolism and anabolism. Catabolism is the breaking down of complex molecules to form simpler ones and often times during the process, release energy. The release of energy is related to the disruption of chemical bonds. One of the important types of catabolic reactions is called hydrolysis. Hydrolysis is the chemical breakdown of a compound due to reaction with water, so a water molecule is added to breakdown a larger molecule into smaller molecules or subunits. So, hydrolysis of sucrose, or table sugar, breaks the molecule into the smaller molecules of glucose and fructose. Hydrolysis of protein breaks it down into smaller molecules of amino acids, and hydrolysis of a fat molecule breaks it down into its smaller subunits of glycerol and fatty acid molecules. Some of the energy released by catabolism is heat energy that keeps the body warm, and much of the energy released is transferred to a molecule called adenosine triphosphate or ATP. Anabolism describes the many chemical reactions that take place to build larger, more complex molecules from smaller subunits. These reactions require energy, which often comes from the breakdown of atp, which was just mentioned. One of the important types of anabolic reactions is called dehydration synthesis. In dehydration synthesis, water is removed as the larger molecules are formed. Anabolic reactions use energy to form larger carbohydrates, fats or lipids, and fuse amino acids together. An example of this is when 2 amino acids join together to form what is called a peptide bond. A peptide bond is when the carboxyl or carbon, oxygen, hydrogen, hydrogen group of one amino acid bonds with the amino nitrogen, hydrogen, hydrogen group of another amino acid, as you can see here (on screen). This is done through a dehydration synthesis reaction, as the amino group involved in the bond loses a hydrogen atom, and the carboxyl group involved in the bond loses an oxygen and hydrogen. So, the peptide bonding results in the release of a water h2o molecule. More amino acids can link in, again releasing water molecules, and form what is called a polypeptide chain, which leads to the production of a protein molecule.
Views: 7247 Whats Up Dude
Four levels of protein structure | Chemical processes | MCAT | Khan Academy
 
08:49
The four levels of protein structure are primary, secondary, tertiary, and quaternary. It is helpful to understand the nature and function of each level of protein structure in order to fully understand how a protein works. By Tracy Kovach. Created by Tracy Kim Kovach. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/chemical-processes/amino-acids-peptides-proteins-5d/v/conformational-stability-protein-folding-and-denaturation?utm_source=YT&utm_medium=Desc&utm_campaign=mcat Missed the previous lesson? https://www.khanacademy.org/test-prep/mcat/chemical-processes/amino-acids-peptides-proteins-5d/v/classification-amino-acids?utm_source=YT&utm_medium=Desc&utm_campaign=mcat MCAT on Khan Academy: Go ahead and practice some passage-based questions! About Khan Academy: Khan Academy offers practice exercises, instructional videos, and a personalized learning dashboard that empower learners to study at their own pace in and outside of the classroom. We tackle math, science, computer programming, history, art history, economics, and more. Our math missions guide learners from kindergarten to calculus using state-of-the-art, adaptive technology that identifies strengths and learning gaps. We've also partnered with institutions like NASA, The Museum of Modern Art, The California Academy of Sciences, and MIT to offer specialized content. For free. For everyone. Forever. #YouCanLearnAnything Subscribe to Khan Academy’s MCAT channel: https://www.youtube.com/channel/UCDkK5wqSuwDlJ3_nl3rgdiQ?sub_confirmation=1 Subscribe to Khan Academy: https://www.youtube.com/subscription_center?add_user=khanacademy
Views: 603998 khanacademymedicine
Peptide synthesis
 
36:31
In organic chemistry, peptide synthesis is the production of peptides, which are organic compounds in which multiple amino acids are linked via amide bonds, also known as peptide bonds. The biological process of producing long peptides is known as protein biosynthesis. This video is targeted to blind users. Attribution: Article text available under CC-BY-SA Creative Commons image source in video
Views: 811 Audiopedia
Peptide bond formation and Amino Acid structure problem
 
06:29
This video includes a basic discussion of the peptide bond. The video also includes one sample problem, which shows a potential exam style questions involving a drawing of a tetrapeptide.
Views: 38916 FortuneFavorsPrep
4.  Kevin Ahern's Biochemistry - Protein Structure I
 
43:55
1. Contact me at [email protected] / Friend me on Facebook (kevin.g.ahern) 2. Download my free biochemistry book at http://www.davincipress.com/freeforall.html 3. Take my free iTunes U course at https://itunes.apple.com/us/course/biochemistry/id556410409 4. Lecturio videos for medical students - https://www.lecturio.com/medical-courses/biochemistry.course 5. Course video channel at http://www.youtube.com/user/oharow/videos?view=1 6. Check out all of my free workshops at http://oregonstate.edu/dept/biochem/ahern/123.html 7. Check out my Metabolic Melodies at http://www.davincipress.com/ 8. My courses can be taken for credit (wherever you live) via OSU's ecampus. For details, see http://ecampus.oregonstate.edu/soc/ecatalog/ecourselist.htm?termcode=all&subject=BB 9. Course materials at http://davincipress.com/bb450.html Highlights 1.The sequence of amino acids in a protein is ultimately responsible for all of the properties a protein has. The sequence of amino acids of a protein is referred to as its primary structure. 2. Peptide bonds form resonance structures such that the bond itself behaves like a double bond. Double bonds cannot rotate (unlike single bonds) and thus they define a plane. Alpha carbons on either side of a peptide bond are generally arranged in a trans configuration (about 10,000 trans to one cis), except when proline is involved. Peptide bonds involving proline favor the trans by about a 100 to 1 ratio. 3. The bonds around the alpha carbon (the carbon bonded to both an amino group and a carboxy group) can both rotate, however, because they are single bonds. One can thus describe a polypeptide as a series of planes separated by an alpha carbon, with the planes each being rotated a certain number of degrees relative to the alpha carbon. If we think of the alpha carbon as being in between two planes, then the plane on the left can rotate (theoretically) 360 degrees and the plane on the right can also theoretically rotate 360 degrees. 4. The Indian scientist, Ramachandran, recognized that not all rotations would be theoretically feasible because steric hindrance would preclude some rotational positions. He plotted theoretical rotations and calculated which of these angles would provide stable structures. The regions of stability turn out to be regions of known stability from protein structures that have been determined. 5. The secondary structure of a polypeptide refers to regular/repeating structure(s) arising from interactions between amino acids that are relatively close together in primary sequence. This means less than 10 amino acids away. 6. One protein secondary structure that is stable in both real proteins and theoretical ones (Ramachandran plots) is the alpha helix. Alpha helices are one type of secondary structure and form coils. 7. Hydrogen bonds are primary forces stabilizing secondary structures. In alpha helices, carbonyl oxygen from a peptide bond forms a hydrogen bond with an amine nitrogen of another peptide bond four amino acids distant. 8. Certain amino acids with simple side chains, such as alanine, are very favorable for formation of alpha helices, whereas bulky (tryptophan) or cyclic (proline) amino acids tend to disrupt alpha helices. Thus, one can reasonably accurately predict from an amino acid sequence which regions of a protein sequence will exist as alpha helices and which will not. 9. Another type of common secondary structure commonly found in protein is the beta strand, which consists of amino acid backbones in a V shape. 10. Beta sheets arise from arrangement of beta strands. These arise from interactions (hydrogen bonds) between beta strands (parallel or antiparallel), such that the carbonyl oxygen of one side interacts with the amine hydrogen with the other. 11. Essential features of proteins that are essential for their overall structure are turns. Turns interrupt secondary structure (alpha helices and beta strands) and often involve proline and glycine residues. 12. Another type of fibrous protein is collagen, the most abundant protein in your body. It contains three intertwined helices comprised of abundant repeating units of glycine, proline, and hydroxylproline 13. Hydroxylation of proline is a post-translational modification (occurs after the protein is made) and the hydroxyls are placed there in a reaction that uses vitamin C. 14. The hydroxyls of hydroxyproline can react with other, forming covalent cross-links that make the collagen fibers more sturdy.
Views: 12028 Kevin Ahern
5 Anti-Aging Skincare Myths Busted | Jar Packaging? Layering Acids? Peptides?
 
14:23
⬇️ Links Below: Click SHOW MORE ⬇️ SUBSCRIBE: http://bit.ly/2s1YyCV Sunscreen Indoors: UVA Radiation: https://www.skincancer.org/prevention/uva-and-uvb Jar Packaging: https://www.cosmeticsbusiness.com/news/article_page/Stability_of_cosmetic_products_shelf_life_or_PAO/128683 https://chemistscorner.com/how-to-stability-test-a-cosmetic-formula/ Ingredient Stability: "Niacinamide ... is stable in the presence of heat and light." Source: https://www.paulaschoice.com/ingredient-dictionary/skin-soothing/niacinamide.html "Niacinamide is a stable and water-soluble form of vitamin B3" Source: https://www.ncbi.nlm.nih.gov/pubmed/29533537 Glycolic Acid: page 7: https://www.fda.gov/media/101373/download Peptides: "research and industry stabilized the peptides by loading them into proteins, and then encapsulated the stabilized peptides into liposomes. The finished product is a stable microemulsion which is ready for formulating.” Source: https://www.bulkactives.com/product/category/peptides Matrixyl 3000: page 4: https://cdn.shopify.com/s/files/1/0026/8317/5001/files/sds_matrixyl_3000_20170802.pdf?10946345458668565309 "Ferulic acid stabilizes a solution of vitamins C and E" Source: https://www.ncbi.nlm.nih.gov/pubmed/16185284 "Reducing the acidity of L-ascorbic acid to a pH below 3.5 is an effective method of improving its stability and permeability." Source: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5605218/ Vitamin C + Niacinamide: "nicotinic acid—the undesirable by-product of niacinamide and vitamin C—becomes an issue only when the niacinamide and vitamin C are combined in a high-temperature environment for a long time." Source: https://www.paulaschoice.com/expert-advice/skincare-advice/myths/can-niacinamide-and-vitamin-c-be-used-together.html?fdid=myths LabMuffin Beauty Science on YouTube: https://www.youtube.com/channel/UCg6P323bLV4zMSWFqFhvWMg Kind of Stephen: https://kindofstephen.com https://kindofstephen.com/can-you-use-niacinamide-and-vitamin-c-ascorbic/ Vitamin C/AHAs + Peptides: Peptide Bonds: http://www.phschool.com/science/biology_place/biocoach/bioprop/peptide.html "peptide (AKA amide) bonds which are pretty strong bonds. Typically this requires something like an enzyme ... or very harsh conditions such as boiling in concentrated acid for a long time." https://www.physicsforums.com/threads/will-all-proteins-fall-apart-by-exaggerated-heat.685477/ "AHAs are a group of weak acids typically derived from natural sources. . . ." Source: https://health.ucdavis.edu/publish/news/research/6853 Retin-A Overview/Efficacy/Safety: https://lpi.oregonstate.edu/mic/health-disease/skin-health/vitamin-A#topical-application Retin-A Skin Thinning: "Retin A and other retinoids do NOT thin your skin over time. They DO thin slightly the outer dead layer (the stratum corneum)" Source: https://www.skintour.com/q-and-a/does-retin-a-or-other-retinoid-creams-thin-your-skin-over-time/ Retin-A skin thickening: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2880508/ "Tretinoin treatment produced a marked increase in the viable epidermal thickness" Source: https://www.sciencedirect.com/science/article/pii/019096229370147L Rosacea: https://www.aad.org/public/diseases/acne-and-rosacea/rosacea#causes MY AMAZON SHOP: https://www.amazon.com/shop/hotandflashy My Discount Codes: *********************************** Curology Prescription Tretinoin: http://bit.ly/2BPCbWp  First Month Free! Timeless Skincare: https://www.timelessha.com Use code hf5off for $5 Off your order! Maelove: http://bit.ly/2x3sGOG  1st Order get 10% Off + Free Shipping with code angiefan Repeat customers get 7% Off + Free Shipping with code goangie Today's Makeup: *********************************** Milk Makeup Hydro Grip Primer: http://bit.ly/2ZBu3SI Estee Lauder Double Wear Foundation (3N1): http://bit.ly/2J3L9Rc Charlotte Tilbury Hollywood Flawless Filter in “4 Medium”: http://bit.ly/2OM5JvB Buxom Wanderlust Primer-Infused Blush in Seychelles: http://bit.ly/2DwoawW Fenty Beauty Amplifying Eye Primer: http://bit.ly/2Ud3akn Dior 5 Couleurs Eyeshadow Palette: http://bit.ly/2hiqH5B Sephora 12 Hr. Contour Eyeliner Pencil in “Lavender Fields”: http://bit.ly/1UDsfSL Marc Jacobs Highliner Gel Eye Crayon in In The Buff & (Iron)y: http://bit.ly/2LcwG4P Urban Decay Double Down Brow Putty in Taupe Trap: http://bit.ly/2DDL3O0 Urban Decay Brow Finish in Ozone: http://bit.ly/2SA039P Buxom Full On Lip Cream in “Dolly” & “Hot Toddy”: http://bit.ly/2gzwS3e Nail Polish: Essie "Teacup Half Full" Necklace: http://bit.ly/2Pfdevc Bracelet: http://bit.ly/2Kv3Hyi Top: http://bit.ly/2L3Ez20 All Rights Reserved © 2019, Hot & Flashy, LLC FTC: Not Sponsored. All opinions are always 100% honest and my own. Links are affiliate links. If you click a link and buy something, I receive a commission for the sale. It doesn't cost you anything extra and you are free to use the link or not as you choose. If you do use my links, I appreciate your support.
Views: 103541 HotandFlashy
Nucleotides and phosphodiester linkages
 
11:03
nucleotides and phosphodiester linkages
Views: 45969 Carol St.Angelo
Protein Structure III
 
49:34
This course is part of a series taught by Kevin Ahern at Oregon State University on General Biochemistry. For more information about online courses go to http://ecampus.oregonstate.edu/ http://www.youtube.com/playlist?list=PL850269AA28EF394A 1. Another type of fibrous protein is collagen, the most abundant protein in your body. It contains three intertwined helices comprised of abundant repeating units of glycine, proline, and hydroxylproline 2. Hydroxylation of proline is a post-translational modification (occurs after the protein is made) and the hydroxyls are placed there in a reaction that uses vitamin C. 3. The hydroxyls of hydroxyproline can react with other, forming covalent cross-links that make the collagen fibers more sturdy. 4. Tertiary structure relates to interactions between amino acids in a protein that are not close in primary sequence. These interactions are made possible by folding to the protein chain to bring the distant amino acids closer together. 5. Tertiary structure is stabilized by disulfide bonds, ionic interactions, hydrogen bonds, hydrophilic, and hydrophobic interactions. Disulfide bonds are the strongest forces holding tertiary structure together, as they are covalent bonds. 6. Most proteins that are in cells are globular in nature. 7. Myoglobin is protein that acts as an oxygen 'battery', storing oxygen in muscles for when it is needed. Myoglobin contains a heme group that contains iron. Heme is a 'prosthetic group', which refers to a non-amino acid containing group that binds to a protein and augments its function. 8. Amino acid residues in myoglobin are arranged such that hydrophilic (and what your book calls ionic) amino acids are arranged on the outside and hydrophobic amino acids are largely arranged on the inside. 9. Porin is a membrane protein. Proteins embedded in membranes often have external amino acids that are hydrophobic so they can interact with the non-polar portions of membranes. Porin, in addition, has a hole in the center that allows water to pass through it. The amino acids in porin are arranged with non-polars outside and polars inside. 10. Quaternary structure of proteins relates to the interactions between separate polypeptide chains within the protein. The word polypeptide refers to a polymer of amino acids. A protein may contain one or more polypeptides and is folded and may be covalently modified. 11. Hemoglobin (and many other proteins) have multiple polypeptide subunits. Interactions between the subunits include disulfide bonds, ionic interactions, hydrogen bonds, hydrophilic, and hydrophobic interactions. Modification of the quaternary structure of a protein may have the same effects as modification of its tertiary structure - alteration of its function/activity. 12. Ribonuclease is an enzyme that degrades RNA. It is unsually stable. For example, it can be heated up to break its hydrogen bonds, but when cooled down, the enzyme still is active, meaning it has assumed its original shape. 13. Denaturation is a word that means the tertiary and/or quaternary structure of a protein is disrupted. RNase has disulfide bonds that help it to remain resistant to denaturation. 14. Some chemicals, such as mercaptoethanol, can reduce the disulfides (between cysteine residues) in proteins to sulfhydryls. In the process of transferring electrons to the cysteines, the sulfhydryls of mercaptoethanol become converted to disulfides. Treatment of RNase with mercaptoethanol reduces RNAse's disulfides to sulfhydryls. Subsequent treatment of RNase with urea disrupts hydrogen bonds and allows the protein to be denatured. 15. Interestingly, removal of the mercaptoethanol and urea from the solution allows RNase to refold slightly, and regaining activity. Clearly, the primary sequence of this protein is sufficient for it to be able to refold itself to the proper configuration. (Note many proteins do NOT do this, however) More interesting, though about ribonuclease is the fact that is one denatures it with urea and mercaptoethanol and then removes the urea, but leaves a tiny amount of mercptoethanol, a lot more enzyme is converted to the active form. The question I asked in class was why. The answer is as follows - RNase has many disulfide bonds and these appear to be key to helping the enzyme to fold. If one removes the urea and the mercaptoethanol simultaneously, the disulfides come back together randomly. Only a small percentage of these random joinings are the right ones that lead to correctly folded RNase. On the other hand, if one keeps the disulfides reduced with a little mercaptoethanol, the hydrogen bonds can reform first, starting part of the folding process that results in the proper alignment of cysteine residues and proper formation of disulfides. Consequently, much more properly folded protein is produced.
The Peptides Podcast: Everything You Need To Know About Anti-Aging, Muscle Gain, Fat Loss & Recover
 
01:14:43
Listen to the full episode here https://bengreenfieldfitness.com/peptidepodcast I receive plenty of questions about peptides and SARMs, including: -How do peptides work? -What is the safety/side effects of peptides? -What are the best anti-aging peptides? -What are the best fat loss and muscle gain peptides? -What are the best recovery peptides? -What peptides work for cognition and neural enhancement? -How do you properly mix and administer peptides? -Do peptides need to be "cycled"? My guest on today's show, Jean-François Tremblay, comes highly recommended by former podcast guest and regenerative medicine physician Dr. Matt Cook as one of the world's leading experts on the wonderful world of peptides and SARMs. Dr. Tremblay studied Exercise Physiology, Biochemistry and Pharmacology. He has been investigating (in theory and in practice) peptides and SARMs since the 1990's and now makes peptides his main research subject. He has developed a wealth of expertise on peptides and SARMs and their practical applications in sports performance, anti-aging and health in general. During my discussion with Jean-François Tremblay, you'll discover: -The science of peptides and how they work...5:55 Amino acids linked together Growth hormone contains 191 amino acids When enough peptides link together, it becomes a protein Demistifying some of the myths surrounding peptides: They must be refrigerated at all times (only for certain peptides) Methionine bonds Most peptides are long chain, stable at room temp, More sensitive to light than heat (degradation more likely result of overexposure to light than heat) The "local effect" (BPC 157 and TB 500) -The pros and cons of various means of injecting peptides...15:15 Intra-nasal absorption is not 100%; however, what is injected has a better chance of reaching the brain Semax: Originally researched in USSR during the Cold War Russians are meticulous in their research; however, lacking in ethics Icarus documentary Researched on humans before other animals; published only after testing on animals -Peptide safety and side effects of use...21:30 Worst-case scenario of "overdosing" on peptides is that it simply doesn't work; no notable negative side effects Not the case with nootropics; you're messing with the brain's chemistry Bottom line: Don't throw caution to the wind. Be aware of proper dosages and administer correctly to the best of your knowledge -Legality and sourcing issues with peptides...32:15 99% of them come from China (even if the label says "Made in the USA") Chinese government dictates who produces what, such as peptides Chinese company released a growth hormone which was very effective, then replaced it with another (under the same name) that had negative side effects Scandinavian company was dishonest about dosage of melanotan (5 mg when advertised as 10 mg) There are only a couple of sources, albeit distributed by many different brands The bacteriostatic water included with the peptide should be crystal clear when it's added There's a reason for the high cost: equipment, repairs, etc. -Whether peptides need to be "cycled" in their use...44:00 Some, yes. It depends on the peptide Effect of BPC-157 lasts around 6 hours Effect of TB-500 lasts 10-15 days; but it's out of your system in 12 hours -Recommended anti-aging peptides...49:30 Epitalon The effects are not as immediate as peptides such as BPC-157 MOTS-c Humanan -The best peptides for fat loss...58:38 There is no "magic pill" Take care of the low hanging fruit: exercise, diet, etc. Tesamorelin (Egrifta) CJC-1295 (no dac version) -Recommended peptides for muscle gain...1:02:45 Nothing for non-competitive use Requires strict discipline and patience; marginal results at best -Jean-François' peptide regimen...1:04:51 Epitalon DSIP (affects the delta phase of sleep only) TB-500 (once a month) BPC-157 (once every couple of months) Thymus (timalin or vilon) twice a year Semax very occasionally -And much more... Resources from this episode: -Dr. Seed's Oral BPC-157 (use code BEN for 15% off ) -My first podcast with Dr. Matt Cook -My second podcast with Dr. Matt Cook -My podcast with Jay Campbell -GlobalDro -CanLab -Icarus documentary Episode Sponsors: -Kion: My personal playground for new supplement formulations. Ben Greenfield Fitness listeners receive a 10% discount off your entire order when you use discount code: BGF10.   -JOOVV: After using the Joovv for close to 2 years, it's the only light therapy device I'd ever recommend. Give it a try: you won't be disappointed. Order using my link and receive nice bonus gift with your order!   -Thrive Market: Organic brands you love, for less. Your favorite organic food and products. Fast and free shipping to your doorstep. Receive 25% off your order when you use my link!   -Birdwell Beach Britches: Quality is our Gimmick isn’t just our slogan, it’s a commitment we honor with every stitch we sew. 100% money back guarantee. Get 10% off your order, PLUS free shipping on any
Proteolysis
 
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Proteolysis -This lecture explains about the protein degradation process by ubiquitination. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching Proteolytic cleavage breaks down proteins in meals extracellularly into smaller peptides and amino acids so that they could also be absorbed and utilized by an organism. Proteins in cells are also constantly being broken down into amino acids. This intracellular degradation of protein serves a number of functions - it removes damaged and irregular protein and avoid their accumulation, and it additionally serves to keep watch over mobile tactics by way of removing enzymes and regulatory proteins that are not needed. The amino acids may then be reused for protein synthesis. The intracellular degradation of protein is also finished in two methods - proteolysis in lysosome, or a ubiquitin-dependent procedure which pursuits unwanted proteins to proteasome. The autophagy-lysosomal pathway is almost always a non-selective process, but it may emerge as selective upon hunger whereby proteins with peptide sequence KFERQ or equivalent are selectively broken down. The lysosome comprises a gigantic quantity of proteases equivalent to cathepsins. The ubiquitin-mediated approach is selective. Proteins marked for degradation are covalently linked to ubiquitin. Many molecules of ubiquitin is also linked in tandem to a protein destined for degradation. The polyubiquinated protein is detailed to an ATP-elegant protease problematic, the proteasome. The ubiquitin is launched and reused, while the particular protein is degraded. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page Animation source: Discover Biology, Core 3rd Edition, W W Norton and company Link- http://www.wwnorton.com/college/biology/discoverbio3/core/content/index/animations.asp
Views: 24099 Shomu's Biology
Amino Acids and Proteins: How to draw Alpha Amino Acids and Primary Structure of Proteins
 
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Alpha Amino Acids Amino acids are the building blocks of proteins. The structure of the alpha amino acid that we need to know in A Level Chemistry is as shown: alpha amino acid general structure We can remember the structure of alpha amino acid by these 3 positions: 1. amine group -NH2 2. alpha carbon with a R group 3. acid group -COOH Different amino acids have the same basic structure and only differ in the R group. Hence it is important for us to identify the R group so that we can identify the amino acid. Primary Structure of Proteins The unique sequence of amino acids linked via peptide bonds to form a polypeptide chain will give the primary structure of proteins. The structure of proteins is also in a standard format which is very similar to that of the amino acid: amino acid protein general structure So if we have a tripeptide -Asp-Ser-Val- to draw, we simply duplicate the structure 3 times and substitute each R group with the R group of the respective amino acid. tripeptide Asp-Ser-Val Learn how to draw alpha amino acids and primary structure of proteins in this video lesson! Topic: Nitrogen Compounds, Organic Chemistry, JC, H2, A Level Chemistry, Singapore Found this video useful? Please LIKE this video and SHARE it with your friends! Any feedback, comments or questions to clarify? Suggestions for new video lessons? Drop them in the COMMENTS Section, I would love to hear from you! You can also view this video lesson with screenshots and detailed explanation at https://chemistryguru.com.sg/how-to-draw-amino-acids-and-proteins Do check out the following for more video lessons: Organic Chemistry Videos at https://chemistryguru.com.sg/a-level-organic-chemistry-video-lessons A Level Chemistry Videos at https://chemistryguru.com.sg/a-level-chemistry-video-lessons If you are looking for H2 Chemistry Tuition, do consider taking up my classes at Bishan. More info at https://chemistryguru.com.sg/ -~-~~-~~~-~~-~- Please watch my latest video: "Determine Feasibility of Redox Reaction" https://www.youtube.com/watch?v=ZWt2Yc1iPOA -~-~~-~~~-~~-~-
Views: 654 Chemistry Guru
Organic Chemistry 51C. Lecture 18. Amino Acids, Peptides, and Proteins.
 
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UCI Chem 51C Organic Chemistry (Spring 2012) Lec 18. Organic Chemistry -- Amino Acids, Peptides, and Proteins -- View the complete course: http://ocw.uci.edu/courses/chem_51c_organic_chemistry.html Instructor: James S. Nowick, Ph.D. License: Creative Commons BY-NC-SA Terms of Use: http://ocw.uci.edu/info. More courses at http://ocw.uci.edu Description: This is the third quarter course in the organic chemistry series. Topics covered include: Fundamental concepts relating to carbon compounds with emphasis on structural theory and the nature of chemical bonding, stereochemistry, reaction mechanisms, and spectroscopic, physical, and chemical properties of the principal classes of carbon compounds. Organic Chemistry 51C is part of OpenChem. http://ocw.uci.edu/collections/open_chemistry.html Recorded on June 6, 2012 Index of Topics: 2:49-Amino Acid Structure 5:55-Examples of Polypeptides 12:18-20 Common Amino Acids 17:03-Polar & Charged Amino Acids 22:35-Chemical Synthesis of Peptides and Proteins 27:49-Protecting Groups 31:54-DCC 40:07-Boch Deprotection Mechanism 42:44-Special Amino Acids 43:33-Additional Protecting Groups 46:42-Modern Solid-Phase Peptide Synthesis 54:20-Boch Opolystyrene Example 59:54-Fmoc Group Required attribution: Nowick, James S. Organic Chemistry 51C (UCI OpenCourseWare: University of California, Irvine), http://ocw.uci.edu/courses/chem_51c_organic_chemistry.html [Access date]. License: Creative Commons Attribution-ShareAlike 3.0 United States License (http://creativecommons.org/licenses/by-sa/3.0/us/deed.en_US).
Views: 28238 UCI Open
Biochemistry- Making a Polypeptide Chain
 
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This is the first part of making a polypeptide chain. Two amino acids combine, with water leaving (dehydration), forming a polypeptide with a polypeptide bond linking the two joined amino acids.
Views: 26032 Susanne Whitcomb
Ahern's BB 350 at OSU - 14. Nucleic Acids
 
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Contact me at [email protected] Facebook friend me at https://www.facebook.com/kevin.g.ahern 1. Arachidonic acid is a 20 carbon fatty acid (eicosanoid) with 4 double bonds. It is a precursor of the prostaglandins. Prostaglandins are molecules that are involved in pain and swelling, among other phenomena in the body. The enzyme catalyzing their synthesis is called PGH Synthase, Prostaglandin Synthase, or Cyclooxygenase (COX). COX enzymes (there are several) are inhibited by aspirin and ibuprofen. These are known as NSAIDs (Non-steroidal anti-inflammatory drugs). 2. Compounds related to prostaglandins include leukotrienes, which are involved in allergic responses and may also be involved in asthma, and thromboxanes, which are derived from prostaglandins and play roles in the stickiness of blood platelets. Nucleic Acids 1. Nucleic acids are composed of building blocks called nucleotides. Nucleotides have three components - a sugar (ribose or deoxyribose), at least one phosphate, and a nitrogenous base (adenine, guanine, thymine, cytosine, or uracil). 2. DNA differs from RNA in that DNA contains the sugar deoxyribose instead of ribose and DNA contains the base thymine, whereas RNA substitutes the base, uracil. 3. The bases in nucleic acids are divided into two groups. Pyrimidines include cytosine, thymine, and uracil. Purines include adenine and guanine. 4. A nucleoside differs from a nucleotide in that a nucleoside only has a sugar and a base. It does NOT have phosphate. 5. Note the numbering of the sugar in a nucleotide. The phosphate goes on carbon number 5. the differences between ribose and dexoyribose are on carbon #2, where ribose contains a hydroxyl, but deoxyribose contains only a hydrogen. 6. The 5' end of a nucleic acid is the end of the nucleic acid that has a free 5' end (no bond). The 3' end of a nucleic acid is the other end of the nucleic acid and it too is not tied up in a bond. All other 5' and 3' ends are joined together in phosphodiester bonds. 7. The "backbone" of a nucleic acid is composed of alternating phosphates and sugars and the bond linking them is called a phosphodiester bond. Phosphodiester bonds are to nucleic acids what peptide bonds are to proteins. The bases are NOT part of the backbone and in a DNA molecule are internal to the surrounding backbone. 8. The double helix of DNA was discovered by Watson, Crick, and Franklin in 1953. The most common form is called the B-form. It consists of two strands oriented in an anti-parallel fashion (slide 10) arranged in a right-handed fashion. Bases are located on the inside such that adenine forms 2 hydrogen bonds (pairs) with thymine and cytosine forms 3 hydrogen bonds with guanine. 9. Other forms of DNA duplexes include the A form (right handed also and also the form of double stranded RNA) as well as the Z form of DNA (left handed). 10. Supercoiling is one aspect of the structure of DNA. Bacterial chromosomes are circular, so if twists are inserted (or removed) from standard B DNA, supercoiling arises.
Views: 2561 Kevin Ahern
Inside the Brain: Unraveling the Mystery of Alzheimer's Disease [HQ]
 
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This 4-minute captioned video shows the intricate mechanisms involved in the progression of Alzheimer's disease in the brain. http://www.nia.nih.gov Permission to use ADEAR materials is not required. When you use our materials in print, on the Web, or in a video or audio format, we simply request that you credit the "Alzheimer's Disease Education and Referral Center, a service of the National Institute on Aging." The human brain is a remarkable organ. Complex chemical and electrical processes take place within our brains that let us speak, move, see, remember, feel emotions and make decisions. Inside a normal healthy brain, billions of cells called neurons constantly communicate with one another.They receive messages from each other as electrical charges travel down the axon to the end of the neuron. The electrical charges release chemical messengers called neurotransmitters. The transmitters move across microscopic gaps, or synapses, between neurons. They bind to receptor sites on the dendrites of the next neuron.This cellular circuitry enables communication within the brain. Healthy neurotransmission is important for the brain to function well. Alzheimer's disease disrupts this intricate interplay. By compromising the ability of neurons to communicate with one another, the disease over time destroys memory and thinking skills. Scientific research has revealed some of the brain changes that take place in Alzheimer's disease. Abnormal structures called beta amyloid plaques and neurofibrillary tangles are classic biological hallmarks of the disease. Plaques form when specific proteins in the neuron's cell membrane are processed differently. Normally, an enzyme called Alpha-secretase snips amyloid precursor protein, or APP, releasing a fragment. A second enzyme, Gamma-secretase, also snips APP in another place. These released fragments are thought to benefit neurons. In Alzheimer's disease, the first cut is made most often by another enzyme, Beta-secretase. That, combined with the cut made by Gamma-secretase, results in the release of short fragments of APP called Beta-Amyloid. When these fragments clump together, they become toxic and interfere with the function of neurons. As more fragments are added, these oligomers increase in size and become insoluable, eventually forming Beta-Amyloid plaques. Neurofibrillary tangles are made when a protein called tau is modified. In normal brain cells, tau stabilizes structures critical to the cell's internal transport system. Nutrients and other cellular cargo are carried up and down the structures called microtubules to all parts of the neuron. In Alzheimer's disease, abnormal tau separates from the microtubules, causing them to fall apart. Strands of this tau combine to form tangles inside the neuron, disabling the transport system and destroying the cell. Neurons in certain brain regions disconnect from each other and eventually die, causing memory loss. As these processes continue, the brain shrinks and loses function. We now know a great deal about changes that take place in the brain with Alzheimer's disease, but there is still much to learn. What other changes are taking place in the aging brain and its cells and what influence do other diseases, genetics, and lifestyle factors have on the risk of developing Alzheimer's disease as the brain and body age? Scientific research is helping to unravel the mystery of Alzheimer's and related brain disorders As we learn more, researchers move ever closer to discovering ways to treat and ulimately prevent this devestating, fatal disease.
Views: 709864 Alzheimer Universal
Is Elastin A Structural Protein?
 
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Biopolymers elastin major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly recover completely. Htmlelastin is a major protein component of tissues that require elasticity such as arteries, lungs, bladder, skin and elastic ligaments cartilage. Each fibrous protein primary structure of is the sequence amino acids in a polypeptide chain. In bone, tendon & cartilage) elastin ( elastic fibers of connective tissues) collagens are the main structural component tissue and they protein has little structure individual proteins crosslinked into a Structural biochemistry fibrous wikibooks, open what is elastin? Definition explanation video lesson what's difference between collagen elastin? Elastin wiley online library. Structural biochemistry proteins fibrous wikibooks, open what is elastin? Definition & explanation video lesson what's the difference between collagen and elastin? Elastin wiley online library. Elastin polypeptide chains are cross linked together to form rubberlike, elastic fibers human bodies contain hundreds of proteins that perform specific functions. Collagen of bones, elastin in ligaments, keratin hair and horry tissues fibroin silk 28 mar 2017 official full text paper (pdf) the structures their function. Swollen elastin, could be a triphasic system comprising the protein we focus our discussion on sequence, structure and function of five rubber like elastomeric proteins, resilin, spider silk, abductin colp. Tropoelastin is a 65kda protein that highly cross linked to form an insoluble complex elastin elastic in connective tissue and allows many tissues the body resume their shape after stretching or contracting. Molecular determinant of the 18 feb 2017 collagen and elastin are structural proteins extracellular matrix. Elastin wikipediasigma aldrichbritannica. Microfibrils, of which fibrillin 1 is the major component, are structures present in elizabeth ii. The proteins are all remarkably similar in structure e. Although comparative structures and properties of elastic proteins. The science of elastin elastagenthe structures and their function (pdf download available). Elastin wikipedia a url? Q sigmaaldrich life science biochemicals biochemical products. Collagen is a family of proteins found in animals, so abundant that it 19 nov 2012 collagen and elastin are examples well characterized fibrous serve structural functions the body. Arthur s tatham and hydrophobic interaction a model for the elasticity of elastin. Elastin lacks a regular secondary structure the protein elastin is major structural component of those tissues in cross links are two polyfunctional amino acids, desmosine and tropoelastin fundamental building all. Over time, aging can deplete the skin of these two key proteins 17 feb 2012 it is classed as a fibrous protein because its structural function and relative insolubility in water. Elastin helps skin to return its original position when it is poked or pinched others include fi
Views: 344 Stores
Protein Powders Spiked With Creatine Are A SCAM
 
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► THE BODY TRANSFORMATION BLUEPRINT Science-based muscle building and fat loss system: http://www.BodyTransformationTruth.com ► REALSCIENCE ATHLETICS No B.S, premium quality supplements you can trust: http://www.RealScienceAthletics.com CONNECT WITH ME Blog: http://www.SeanNal.com Instagram: https://www.instagram.com/Sean_Nalewanyj/ Facebook: https://www.facebook.com/SeanNalewanyjOfficial GET YOUR FREE CUSTOM MEAL PLAN http://www.SeanNal.com/free-meal-plan.php TAKE MY ONLINE FITNESS QUIZ http://www.SeanNal.com/quiz-questions.php -------------------------------------------------------------------------------- More Info On Amino Acid Spiking: http://www.SeanNal.com/articles/supplementation/amino-acid-spiking.php Recommended Whey Protein Powders: http://www.SeanNal.com/recommended-whey-protein.php -------------------------------------------------------------------------------- Video Transcript: "Whey Protein Powders With Added Creatine Are A SCAM" Hey guys, Sean Nalewanyj here of BodyTransformationTruth.com, and in this video I’m going to explain why protein powders that add creatine into the mix are a scam and why they should be avoided. Now, this whey protein scam directly relates to the whole issue of "amino acid spiking" which you may have heard about already, I did a post on that a while back which I’ll link in the description box if you want more info, but basically to keep a long story short, whey protein costs have very significantly increased over the past few years, and because a very high percentage of supplement companies are run by people who are primarily interested in making money as opposed to actually producing legitimately high quality products, a lot of these companies are basically taking advantage of loopholes in the system to cut their production costs. Now, along with adding free form l-taurine, l-glycine and glutamine into the powders, mixing in creatine is another amino acid spiking method that’s used, and it’s actually probably the worst form of spiking there is. So how how does this work exactly? Well, I want to keep this short, so without going into all the details, the total protein gram amount that’s listed on a tub of protein powder is based on the total nitrogen content (this is how protein powders are test) and because creatine contains nitrogen bonds, it actually registers as part of the protein total. And not only that but some tests have actually shown that it can register as high as about 140% protein. So if you took a standard 5 grams of creatine per scoop let’s say, that could potentially be artificially adding 7 grams of protein to each serving. So if your protein powder lists 22 grams of protein per scoop but it also contains creatine, it’s possible that that could actually be as low as 15 grams of protein. And because creatine can be safely used at doses even higher than that, it’s possible that some companies are using even more than 5 grams for protein spiking purposes. Creatine is tasteless so you’d have no way of knowing that it’s in there, and most products won’t actually list the creatine amount so you really don’t know what’s going on at all. Now again, why do companies do this? Well, creatine monohydrate is less expensive than whole proteins are, and when you’re moving tens, or hundreds of thousands or millions of units of product, that small amount that you save per tub adds up very big in the overall picture. And it’s actually a “good scam” to run, because creatine is such a recognizable ingredient, a high percentage of lifters use it, so they’ll see it on the label and think, "oh I’m getting 25 grams of protein plus my daily serving of creatine" without realizing that the creatine itself is actually part of the protein total. So, bottom line, creatine is a great muscle building supplement, and I do recommend it, but it has no place in a protein powder and it should be purchased separately. Check the ingredient label on the protein powder that you buy, and if it has creatine listed, or as I talked about before, l-taurine, l-glycine or glutamine peptides, then leave it on the shelf since it is almost certainly a spiked protein powder. There are tons of good quality whey protein products that aren't spiked out there, so I couldn’t possibly list them all, but personally I use Optimum Nutrition 100% Whey and Dymatize Elite Whey at the moment, which are both high quality, legit powders and reasonably priced, and I’ll link those in the description box as well for you.
Views: 15517 Sean Nalewanyj
What is CONDENSATION POLYMER? What does CONDENDSATION POLYMER mean? CONDENSATION POLYMER meaning
 
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What is CONDENSATION POLYMER? What does CONDENDSATION POLYMER mean? CONDENSATION POLYMER meaning - CONDENSATION POLYMER definition - CONDENSATION POLYMER explanation. Source: Wikipedia.org article, adapted under https://creativecommons.org/licenses/by-sa/3.0/ license. Condensation polymers are any kind of polymers formed through a condensation reaction—where molecules join together—losing small molecules as byproducts such as water or methanol, as opposed to addition polymers which involve the reaction of unsaturated monomers. Types of condensation polymers include polyamides, polyacetals and polyesters. Condensation polymerization, a form of step-growth polymerization, is a process by which two molecules join together, resulting in loss of small molecules which are often water. The type of end product resulting from a condensation polymerization is dependent on the number of functional end groups of the monomer which can react. Monomers with only one reactive group terminate a growing chain, and thus give end products with a lower molecular weight. Linear polymers are created using monomers with two reactive end groups and monomers with more than two end groups give three-dimensional polymers which are crosslinked. Dehydration synthesis often involves joining monomers with an -OH (hydroxyl) group and a freely ionized -H on either end (such as a hydrogen from the -NH2 in nylon or proteins). Normally, two or more different monomers are used in the reaction. The bonds between the hydroxyl group, the hydrogen atom and their respective atoms break forming water from the hydroxyl and hydrogen, and the polymer. Polyester is created through ester linkages between monomers, which involve the functional groups carboxyl and hydroxyl (an organic acid and an alcohol monomer). Nylon is another common condensation polymer. It can be manufactured by reacting di-amines with carboxyl derivatives. In this example the derivative is a di-carboxylic acid, but di-acyl chlorides are also used. Another approach used is the reaction of di-functional monomers, with one amine and one carboxylic acid group on the same molecule. The carboxylic acids and amines link to form peptide bonds, also known as amide groups. Proteins are condensation polymers made from amino acid monomers. Carbohydrates are also condensation polymers made from sugar monomers such as glucose (i.e. cellulose or glycogen) and galactose. Condensation polymerization is occasionally used to form simple hydrocarbons. This method, however, is expensive and inefficient, so the addition polymer of ethene (polyethylene) is generally used. Condensation polymers, unlike addition polymers, may be biodegradable. The peptide or ester bonds between monomers can be hydrolysed by acid catalysts or bacterial enzymes breaking the polymer chain into smaller pieces. The most commonly known condensation polymers are proteins, fabrics such as nylon, silk, or polyester.
Views: 2563 The Audiopedia
#21 BB 350 Translation III / Biotechnology I - Kevin Ahern's Biochemistry Online
 
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1. Contact me at [email protected] / Friend me on Facebook (kevin.g.ahern) 2. Download my free biochemistry book at http://biochem.science.oregonstate.edu/biochemistry-free-and-easy 3. Take my free iTunes U course at https://itunes.apple.com/us/course/biochemistry/id556410409 4. Check out my free book for pre-meds at http://biochem.science.oregonstate.edu/biochemistry-free-and-easy 5. Course video channel at http://www.youtube.com/user/oharow/videos?view=1 6. Check out all of my free workshops at http://www.youtube.com/playlist?list=PLlnFrNM93wqyTiCLZKehU1Tp8rNmnOWYB&feature=view_all 7. Check out my Metabolic Melodies at http://www.davincipress.com/metabmelodies.html 8. Take my courses for credit (wherever you live) via OSU's ecampus. For details, see http://ecampus.oregonstate.edu/soc/ecatalog/ecourselist.htm?termcode=all&subject=BB 9. Course materials at http://oregonstate.edu/instruct/bb350 Lecture Highlights Translation 3 1. Post-translational processing of proteins gives them their final structure and properties. One such modification was discussed for insulin. This involves proteolytic cleavage at two places in the insulin precursor, giving rise to a final structure that has two chains held together by disulfide bonds. 2. Proteins do not have long lifetimes in the cell. They are broken down in cells in cellular structures called proteasomes. Proteins targeted for degradation are tagged with the peptide known as ubiquitin. 3. Selenocysteine is a rare amino acid occasionally incorporated into proteins. It is sometimes called the 21st amino acid. It is because of this that trace amounts of selenium are needed in the diet. 4. Proper folding of proteins is important. A complex in E. coli that facilitates proper folding of proteins is the GroES/GroEL complex. Biotechnology 1. Biotechnology employs knowledge of the processes of DNA replication, transcription, and translation to make useful products. 2. Cloning of organisms is one application of biotechnology. 3. The modern era of biotechnology began with the discovery of restriction endonucleases (=restriction enzymes). These are enzymes isolated from bacterial cells that bind to DNA, recognize a specific DNA sequence, and cut at that sequence. 4. Many restriction enzymes recognize specific inverted repeat sequences and cut there. As shown for EcoRI, the cut DNA fragments have overhanging ends called "sticky" that can be used to form base pairs that are useful for putting pieces back together with DNA ligase. 5. In normal bacterial cells, restriction enzymes are paired with an enzyme called a methylase. Methylase puts a methyl group on the sequence the restriction enzyme would otherwise cut. Cellular DNA is protected in this way. Invading virus sequences, however, aren't methylated, so their DNAs get cut by the restriction enzymes. 6. If one piece of a DNA molecule is linked to a foreign DNA molecule, a recombinant molecule is created. If one uses DNA ligase to link a DNA to a circular DNA that replicates in bacteria (called a plasmid), then the foreign DNA will be replicated in the bacterial cells. If the plasmid has a promoter that can control transcription, the plasmid is known as an expression vector. 7. The effciency with which plasmids can be put into cells is about 1 cell in 100000 at the best. Antibiotic resistance (carried in a gene on the plasmid) is a good way of screening for bacterial cells that get a plasmid. This is done by plating bacteria on a plate of agar that contains a specific antibiotic that the plasmid gene gives resistance to. Only cells with the plasmid will grow. 9. When recombinants are made by ligating a foreign DNA into a plasmid, this process too is not very efficient. A method for determining not only which cells get plasmids, but also which cells get plasmids with DNA inserted into them is also desirable. This latter method involves what is called blue-white screeening and it employs the lac-z (beta-galactosidase) gene of E. coli. 10. In blue-white screening, a plasmid contains the following things - antibiotic resistance, origin or replication, and lac-z gene with at least one restriction site in the gene. Researchers cut DNA with the same restriction enzyme as the restriction enzyme site in lac-Z and then ligate the fragments in the presence of the plasmid cut with the same gene. If a plasmid gets an insert into the lac-z gene, the gene doesn't function. If no insert goes into the gene and the plasmid simply re-forms the original gene, lac-z functions. 11. The ligation mixture is transformed into E. coli cells and plated on an antibiotic (to ensure that only cells with plasmids grow) and a compound known as X-gal. X-gal has the property that if the lac-z gene is present, it will cleave it and produce a blue color. If no lac-Z is present, a white color is produced.
Views: 2316 Kevin Ahern
Ahern's BB 350 at OSU - 21. Translation 3 & Biotechnology
 
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Contact me at [email protected] Facebook friend me at https://www.facebook.com/kevin.g.ahern Highlights Translation 3 1. Translation is a target for action of antibiotics. This works because the phenomenon of translation in prokaryotes is different enough from that of eukaryotes that specific inhibitors of prokaryotic translation can be found that have no effect on eukaryotic translation. As a result, prokaryotes can be killed without any effect on eukaryotes taking said antibiotics. One translational inhibitor of prokaryotic translation is the antibiotic puromycin, which acts to prematurely terminate prokaryotic translation at the elongation phase. This happens because puromycin looks like a tRNA and fits into the A (or P) site of the ribosome. In the A site, it can be attached to the growing polypeptid chain, but it is soon released, causing premature termination. In addition, puromycin can bind to the P site of ribosomes and prevents anything from binding there. 2. Eukaryotic mRNAs have a 5' cap and a 3' polyA tail. Eukaryotic translation occurs much like prokaryotic translation, but the factors are differently named. One important difference of eukaryotic translation is that the initiation complex in eukaryotes involves both the 5' cap and the 3' polyA sequence in a looped structure. The 5' cap and 3' poly-A sequence both play roles in helping to increase the stability of eukaryotic mRNAs. 3. Post-translational (= after translation has occurred) processing of proteins gives them their final structure and properties. One such modification was discussed for insulin. This involves proteolytic cleavage at two places in the insulin precursor, giving rise to a final structure that has two chains held together by disulfide bonds. 4. Proteins do not have long lifetimes in the cell. They are broken down in cells in cellular structures called proteasomes. Proteins targeted for degradation are tagged with the peptide known as ubiquitin. 5. Selenocysteine is a rare amino acid occasionally incorporated into proteins. It is sometimes called the 21st amino acid. It is the only modified amino acid in proteins that gets there by direct incorporation rather than post-translational modification. It is because of this that trace amounts of selenium are needed in the diet. 6. Proper folding of proteins is important. A complex in E. coli that facilitates proper folding of proteins is the GroES/GroEL complex, which provides a chamber for a protein to fold in without interference of other proteins during the folding process. Biotechnology 1. Biotechnology employs knowledge of the processes of DNA replication, transcription, and translation to make useful products. 2. The modern era of biotechnology began with the discovery of restriction endonucleases (=restriction enzymes). These are enzymes isolated from bacterial cells that bind to DNA, recognize a specific DNA sequence, and cut at that sequence. 3. Many restriction enzymes recognize specific inverted repeat sequences and cut there. As shown for EcoRI, the cut DNA fragments have overhanging ends called "sticky" that can be used to form base pairs that are useful for putting pieces back together with DNA ligase. 4. Restriction enzymes are bacterial defense systems. In normal bacterial cells, they are paired with an enzyme called a methylase. The function of the methylase is the put a methyl group on the sequence the restriction enzyme would otherwise cut. Cellular DNA is protected in this way. Invading virus sequences, however, aren't methylated, so their DNAs get cut by the restriction enzymes. 5. If one piece of a DNA molecule is linked to a foreign DNA molecule, a recombinant molecule is created. If one uses DNA ligase to link a DNA to a circular DNA that replicates in bacteria (called a plasmid), then the foreign DNA will be replicated in the bacterial cells. If the plasmid has a promoter that can control transcription, the plasmid is known as an expression vector. An expression vector provides a means of using bacteria to transcribe and translate foreign genes.
Views: 1616 Kevin Ahern
Protein structure | tertiary structure of proteins
 
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Protein structure | tertiary structure of proteins - lecture explains the tertiary structure of proteins. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching In this video tutorial, 3 dimensional structure of proteins are described and it also emphasize on how 3D structures form. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page Biochemistry, 4th Edition Donald Voet, Judith G. Voet November 2010, ©2011
Views: 5438 Shomu's Biology
Lecture - 3 Protein Structure - I
 
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Lecture Series on BioChemistry I by Prof.S.Dasgupta, Dept of Chemistry, IIT Kharagpur. For more details on NPTEl visit http://nptel.iitm.ac.in
Views: 151445 nptelhrd
The Molecular Shape of You - Молекулярна форма тебе. (A Capella Science)
 
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Ed Sheeran Parody - A Capella Science. A dot isn't the best way to try to sum up How electrons come and go They are the states of a matter field That follows an equation that Dirac wrote The Schrodinger part of the whole equation Will just lead in sub-c when it expands Now get that Coulomb and add it in with a proton And watch them start to dance As hydrogen it's like "Oh proton I feel your tug Central potential dip down pulling on me But I'm not falling in deep No that would break uncertainty" "Say oh Electrons move too much Slow down your pace and put that orbit on me Come on now follow my lead Come come on now follow my lead Orbitals take the shape they do As stable states of the quantum rules And when a one approaches two They combine and they're bonding Thus hydrogen as a rule Is found in nature as H2 Energy configuring a molecule Diatomically bonding Low high low high low high low high Diatomically bonding (x3) Energy cofiguring a molecule When orbitals take the shape they do One 'n' half spin will give a lepton a twin One up one down in the ground state With S and P in quadruple degeneracy The second shell can be filled up with eight The higher angular powers spread out Like beautiful flowers In middle families they come into play Well here's a carbon with 6e This ain't nothing tricksy But we're gonna make some methane today With hydrogen it's like "Oh atoms I feel your tug Got my electrons bugged out pulling on me Come on now settle around me I'll hybridize to sp3" "Say oh Carbon here's touch Spread out 109.47 degrees Come on now follow our lead Come come on now follow our lead" Molecules take the shape they do Combining states of the quantum rules Like when a shell goes sp2 For sigma pi double bonding And as widely as their purview They spread out in the molecule Look at benzene in a ring they hold it true Aromatically bonding Low high low high low high low high Aromatically bonding (x3) Look at benzene in a ring they hold it true When orbitals take the shape they do Come bond with me baby, come bond (x8) Polymers take the shape they do Combining base-level residues Like RNA's ACGU Look they're hydrogen bonding! Peptides make a chain and group In beta pleat sheets and corkscrews With these secondary links they fold and move They're all over your body Come bond with me baby, come bond (x6) You're a chemical machine It's best you knew That molecules take the shape of you.