BIOL 112 Chapter Notes - Chapter 4.1: Protein Folding, Amine, Side Chain

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27 Sep 2016
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BIOL 112 Full Course Notes
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BIOL 112 Full Course Notes
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Connected by covalent bonds to an amino group (-nh2) , a carboxyl group (- R groups make the letters of the amino acid alphabet distinct from one another. The chemical structures of amino acids are chemically diverse and grouped according to their properties, particularly emphasizing whether they are. Strongly affect how the polypeptide folds and how the 3d shape of the protein looks. Hydrophobic amino acids do not interact w/ water or form h-bonds. At the ph of a cell, r group of the basic amino acid gain proton, the acidic amino acid lose proton. B/c they are charged, they are located on the outside of the folded molecule. Glycine: r group = hydrogen (therefore, not asymmetric like the others because there"s another h atom on the other side) Small size allows for free rotation around the c-n bond: non-polar, increases flexibility of the polypeptide backbone, important in folding of protein.

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