Biochem objectives

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COMPLETED HOMEWORK July 6, 2011  Focus on Essential Amino Acids o R-Groups (Categorizations)  Proteins are polymers of amino acids, with each amino acid residue joined to its neighbor by a specific type of covalent bond (Peptide Bond)  All 20 of the common Amino acids are Alpha Amino Acids. They have a carboxyl group and an amino group bonded to the same carbon atom, which is called the Alpha carbon. The 20 common Amino Acids differ from each other in their side chains, R-Groups.  The Alpha carbon is a chiral center because it is bonded to 4 distinct groups therefore amino acids can have two possible stereoisomers(enantiomers because they are non- superimposable mirror images).  Nonpolar, Aliphatic Amino Acids  Non-polar and Hydrophobic. Tend to cluster together within proteins, stabilizing protein structure by means of hydrophobic interactions.  Glycine-Gly-G  Alanine-Ala-A  Proline-Pro-P  Valine-Val-V  Leucine-Leu-L  Isoleucine-Ile-I  Methionine-Met-M  Aromatic Amino Acids  Are relatively Non-Polar and Hydrophobic. All can participate in Hydrophobic Interactions. The Hydroxl group of Tyrosine can form Hydrogen Bonds  Phenylalanine-Phe-F  Tyrosine-Tyr-Y  Tryptophan-Trp-W  Polar, Uncharged Amino Acids  The most Hydrophillic R-groups.  The R-groups of these amino acids are more sol uble in water and are more Hydrophillic because they contain functional groups that can hydrogen bond with water.  Serine-Ser-S  Threonine-Thr-T  Cysteine-Cys-C

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