KIN217 Lecture Notes - Lecture 2: Electrophoresis, Enzyme, Antibody
15 Sep 2017
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Carbon nitrogen bond in protein is planar (cannot move or rotate) On either side of either carbon or nitrogen, there are rotations therefore different orientations. Always aims to have the r-group pointing outward. Neighboring h-bonds rather than bonds from different proteins. Space fitted model shows compactness of a protein structure. Alpha/beta has nothing to do with molecular structure/chemical significance. Hydrogen"s in interior, r-groups on exterior, pointing to outside. Precisely stacked on top on each other, no coiling. Main fibrous component of skin, teeth etc . Glycine residue the only molecule that fits in inside helix. Now considering disulfide bonds, hydrogen bonds, salt bridges, etc. R-groups far apart on the amino acid, they are close on the secondary structures. Polar structures move to outside, non-polar structures move inside in myoglobin (tertiary example) Example of how weak forces orient themselves in aqueous solution. Glutamic acid residue, pka = 4. 3 (dominates above 4. 3) Lysine residue, pka = 10. 5 (dominates below 10. 5)
