CH369.lecture4 - Acasestudyofprotein Tertiarystructure(3Dstructures L alanine D-alanine bypeptidebonds Peptidebonds Amino terminus N

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A case study of protein  structure and function Myoglobin and hemoglobin
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Tertiary structure (3-D structures) Green Fluorescence Protein
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Proteins contain L-amino acids only L – alanine D-alanine
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Proteins are chains of amino acids linked  by peptide bonds
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Peptide bonds Amino terminus Carboxyl terminus N - terminus C-terminus
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Amino acids, one and three letter codes Amino acid Three letter code One letter code alanine ala A arginine arg R asparagine asn N aspartic acid asp D asparagine or aspartic acid asx B cysteine cys C glutamic acid glu E glutamine gln Q glutamine or glutamic acid glx Z glycine gly G histidine his H isoleucine ile I leucine leu L lysine lys K methionine met M phenylalanine phe F proline pro P serine ser S threonine thr T tryptophan try W tyrosine tyr Y valine val V
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Negatively charged amino acids
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Positively charge amino acids
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Hydrophilic amino acids
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Hydrophobic amino acids
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Polar side chains can ionize at  physiological pH values
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What is the total charge of a peptide 1) His-His-His-His-His-His 2) Glu-Asp-Ala-His-Glu-Arg at pH 5.0? 9.0?
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Cysteine Thiolate anion
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Two cysteines can form a disulfide bond H2
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Peptide bonds link amino acids in  proteins
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R2 R4 Peptide bond geometry C α C α R1 R2 Residue 1 Residue 2 Residue 3 Residue 4 N-terminus C-terminus
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Protein sequencing 1. Protein purification – sample protein should be free of other proteins 2. remove disulfide bonds
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Protein sequencing 3.  protease digestion  – cleave the protein into small fragments
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This note was uploaded on 03/09/2010 for the course CH 369 taught by Professor Kbrowning during the Spring '07 term at University of Texas at Austin.

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CH369.lecture4 - Acasestudyofprotein Tertiarystructure(3Dstructures L alanine D-alanine bypeptidebonds Peptidebonds Amino terminus N

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