BCH210H1 Lecture 3: Lecture 3

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21 Sep 2016
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BCH210H1 Full Course Notes
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BCH210H1 Full Course Notes
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From the rst amino acid to the last. Secondary: this is how the amino acids are arranged into additional conformational states like the alpha helix and beta plated formations. Tertiary: it is the assembly of the secondary structures into a fully functional protein. The alpha helix: it is stabilized by hydrogen bonds. These bonds are in the back bone of the protein itself. Need to pack the side chains and minimize side chain steric clashes. They can either be right handed or left handed. The angle between the adjacent residues is 100. The residues are 1. 5 angstroms in rise or vertical length. Hydrogen bonds face the interior of the helix. This allows the amino acid to be party on the surface and partly buried o na protein. It is formed from two or more chains of amino acids bonded through alternating intermolecular h bonds. Adjacent strands of the b sheet can be parallel or anti parallel.

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