Lec 11 - Chapter 6 Three Dimensional Structure of Proteins...

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Chapter 6 Three Dimensional Structure of Proteins 1. Protein Secondary Structure 2. Protein Tertiary and Quaternary Structure 3. Protein Stability 4. Protein Folding
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Primary structure Secondary structure Tertiary structure Quartenary structure Folding Structure
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Formation of the peptide bond Polypeptide backbone
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Peptide bond — partial double bond character No rotation
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Six atoms of the peptide group lie in a single plane peptide group usually in trans conformation
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Steric hindrance between side groups
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Peptide backbone: a string of beads How does a polypeptide fold up?
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Relative orientation of peptide groups is specified by the φ and ψ angles φ (phi): rotation around C α -N ψ (psi) rotation around C α -C φ and ψ torsion angles or dihedral angles
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When both peptide groups are in the same plane and the polypeptide is stretched out , the torsion angles are defined as 180 ° • Looking from the C α rotating clockwise increases the angle The torsion angles describes how the backbone is folded up Most φ and ψ combinations are not possible
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φ and ψ are 180° φ and ψ are 0°
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allowed
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This note was uploaded on 10/28/2010 for the course CHEM 114A taught by Professor Viadhiu during the Fall '08 term at UCSD.

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Lec 11 - Chapter 6 Three Dimensional Structure of Proteins...

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