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UVM BCOR 103 - Proteins and Protein Structure
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BCOR 103 1st Edition Lecture 3Outline of Last Lecture I. The Evolution of CellsII. Basic Physics and EnergyIII. Basic Chemistry IV. Organic Bio-moleculesOutline of Current Lecture I. Amino AcidsII. The Peptide BondIII. Levels of Protein StructureIV. Protein AlterationsCurrent LectureThere are twenty amino acids commonly used in biological organisms. All have the samebasic structure, an amino group, a single hydrogen atom, a carboxyl group, and an R-group. The R-group stands to mean any sort of substitution. The acidic, basic, and polar amino acids are classified as hydrophilic- lysine, arginine, histidine, serine, threonine, aspartic acid, glutamic acid,asparagine, and glutamine. The Amino acids that contain a ring are considered to be hydrophobic- alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, and tryptophan. The remaining amino acids are classified as “special amino acids” and this is because they are particularly apt at creating specific bonds- cysteine, glycine, and proline. The peptide bond is the one that links amino acids together. Amino acids are the basic structural unit of proteins, when linked together they form a protein. Amino acids are linked by a process called dehydration. The oxygen atom of one carboxyl group of one amino acid links with the two hydrogens present in the amino group of a second amino acid. When the oxygen and hydrogens join, a water molecule is released and the two amino acids are linked. Inversely, peptide bonds can be broken by hydrolysis. Hydrolysis is when water molecules are added to an amino acid chain, breaking them back into individual amino acids.There are four structures of proteins; primary, secondary, tertiary, and quaternary. The primary structure of a protein is just a sequence of amino acids. Primary structures are held together by peptide bonds. Secondary structure proteins form beta-pleated sheets and alpha helices. Secondary structures are held together with hydrogen bonds. Tertiary structures are mainly held together by hydrophobic interactions. Some amino acids, as previously mentioned, are hydrophobic. When hydrophobic amino acids are in a sequence together they can fold to form a hydrophilic surface outside the hydrophobic interior. Not all proteins can form a These notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.quaternary structure. Quaternary structures are when two or more individual proteins condense together. There are five ways that proteins can be altered after they are synthesized. A protein can be linked to a cell membrane by adding a fatty acid tail, this process is call fatty acid acylation. Some proteins have specific modifications that only that protein does. A protein can have a phosphate added to it, called phosphorylation. The N-terminus of a protein can be acetylated to protect it from degrading over time, acetylation. And lastly, a protein can have sugars added to protect the surface, this process is called


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UVM BCOR 103 - Proteins and Protein Structure

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