BISC 330 Spring 2011 Lecture 6

BISC 330 Spring 2011 Lecture 6 - BISC 330L: Biochemistry...

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BISC 330L: Biochemistry Spring Semester 2011 USC Lecture 6: Monday, 24 January 2011 1. More Chapter 2 material… Secondary Structure β strands/sheets Tertiary Structure
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Levels of Protein Structure Primary Structure : Amino acid sequence of polypeptide chain. (Sequence of amino acid residues joined by peptide bonds. Secondary Structure : Regular chain folding held by noncovalent H-bonding between peptide groups, e.g., α helix, β sheet. Tertiary Structure : 3-dimensional folding held by side- chain
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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 α-carbons all lie in same plane) α α α α α
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By building an atomic model of polypeptide chain, Pauling discovered the alpha ( α ) helix, a secondary structure formed .
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“Ball-and stick” model of right-handed a helix formed by L-amino acid residues via H-bonding between peptide groups, as follows: (1) C=O ----H-N (5) (2) C=O ----H-N (6) (3) C=O ----H-N (7) (4) C=O ----H-N (8) (5) C=O ----H-N (9) etc. ..
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Secondary Structure: β strands and β sheets strand + strand = sheets fully extended distance between adjacent a.a. is ~3.5A parallel and anti-parallel β sheets unique H-bonding properties
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BISC 330 Spring 2011 Lecture 6 - BISC 330L: Biochemistry...

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