outline 5 - Biological Sciences 110a, Fall 2011 Lecture...

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Biological Sciences 110a, Fall 2011 Lecture Outline #5: Protein structure reading: Section 2.5, pp 53-74 (54-75) 1. Primary structure the unique sequence of amino acids in a polypeptide chain Frst residue: N-terminus (still has a charged amine group) last residue: C-terminus (still has a charged carboxylate group) 2. Secondary structure any regular arrangement of the main chain most important secondary structures are stabilized by hydrogen bonds side chains not directly involved in structure alpha helices translation 1.5 Å per residue 3.6 residues per turn 5.4 Å between turns beta sheets 3.5 Å between residues 4.7 Å between strands side chains on alternate faces 3. Tertiary structure the overall fold of the polypeptide chain hydrophobic side chains in, hydrophilic out (in general) motifs (supersecondary structures) beta hairpin alpha/alpha (coiled coil) alpha/beta barrel (TIM barrel) reverse turns (not in text) chain reverses direction H-bond between residues 1 and 4 proline common as residue 2
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This note was uploaded on 09/14/2011 for the course BSCI 110A taught by Professor Broadie/patton during the Fall '08 term at Vanderbilt.

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outline 5 - Biological Sciences 110a, Fall 2011 Lecture...

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