BISC401 Study Guide - Midterm Guide: Protein Structure, Ribose, Calmodulin
22 Dec 2016
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Lecture iii: protein structure and function: aa polypeptide/protein primary (covalent peptide bonds btw. Aa"s) secondary (local folding hydrogen bonds btw. Lecture iv: secondary: beta, pleated structure; anti-parallel or parallel, beta turns, type 1, n+1 proline, type 2, tertiary structure, n+2 always find glycine, stabilized by hydrogen bonds, hydrophobic effect, ionic interactions, and van der. Glycine h as an r group; can be used in places where you need a small aa. Cysteine sulfur; where you can make a disulfide bridge. Histidine ring that allows it to accept a proton or donate it. Proline restriction in things it can do because of its shape (side chain) Hydrophobic effect: cannot dissolve in water because they don"t support h bonding with water; so they get clumped together and water forms a sort of shell around it. Structures of aa"s just need to know how they are classified, and which aa"s belong to which classes; not specific r-groups.
