BISC 330 Spring 2010 Lecture 6

BISC 330 Spring 2010 Lecture 6 - BISC330L:Biochemistry...

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BISC 330L:  Biochemistry Spring Semester 2010 USC Lecture:  Monday, 25 January 2010 1.More Chapter 2 material… Secondary Structure  strands/sheets β Tertiary Structure
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Calculating pI of dipeptide For  Ala-Lys , there are  3  ionizable groups: 1) alpha-amino group contributed by Ala -  assign pK 9.6. 2) alpha-carboxylate group from Lys -  assign pK 2.1. 3) side chain amino group from Lys -  assign pK 10.8. pI = (9.9 + 10.8) / 2 =  10.4
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Calculating pI… 2.1 -carboxyl α 9.6 -amino α 10.9 Tyr  R group Low pH 1.0 pH 4-5 pH 10 High pH 12 +1 0 -1 -2 pI = (2.1 + 9.6) / 2 =  5.9
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                   PROTEIN STRUCTURE SUMMARY               rimary Structure : Amino acid sequence of polypeptide chain.      (Sequence of amino acid residues joined by peptide bonds.  econdary Structure : Regular chain folding held by noncovalent      H-bonding between peptide groups, e.g., a helix, b sheet.  ertiary Structure : 3-dimensional folding held by side-chain      interactions between polypeptide chain secondary structures. uaternary Structure : Multi-subunit complex formed by       interactions between tertiary structures of two or more      polypeptide chains. 
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uling suggested that the partial double bond character arises fr sonance between single and double bond structures.
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Fully extended polypeptide chain (peptide groups and a-carbons all lie in same plane) α α α α α
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By building an atomic model of polypeptide chain, L. Pauling 
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BISC 330 Spring 2010 Lecture 6 - BISC330L:Biochemistry...

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