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Lec 2_sept_8_2017.pdf - What makes proteins so versatile 1...

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What makes proteins so versatile? 1. Potential combinations
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What makes proteins so versatile? 2. Flexibility 3. Prosthetic groups 4. Energy changes
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(From Biology Project/University of Arizona)
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The 20 common amino acids are classified by their side chains: Aliphatic Aromatic Non-Polar Polar Charged
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Proline, is the only amino acid in this group in which the side chain forms a covalent bond with the a –amino group. The proline side chain has a primarily aliphatic character; however, it is frequently found on the surfaces of proteins due to its unique structural constraints. The rigid ring of proline is well-suited to those sites in a protein structure where the protein must fold back on itself (so-called ± turns ² ).
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The oxidation of two cysteine side chains yields a disulfide bond. The product of this oxidation is given the name cystine.
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Aspartic acid (p K a = 3.9) and glutamic acid (p K a = 4.2) typically carry negative charges at pH 7. These amino acid residues are often referred to as
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