BCH210H1 Lecture Notes - Lecture 9: Protein Tertiary Structure, Beta Helix, X-Ray Crystallography
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BCH210H1 Full Course Notes
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Ch 2 (q 1(abc), 2(abc), 3, 4, 19b) Lecture 9/12 - intro to proteins and protein structure. Spectroscopic methods estimate percent of secondary structures in proteins. Cannot locate precisely the helical, sheet, turn, and random regions. Unless x-ray or nmr structure determination is performed: renaturation experiments have shown that information for folding into secondary or tertiary structure is coded in the amino acid seq. Combined knowledge of seq and structure can provide insight into protein function. How to predict: minimum energy calculations can locate low energy regions for protein backbone and side chain rotational angles. Residues on the surface have a higher degree of freedom than those buried. These calculations predict the existence of favoured secondary structures: the alpha-helix and beta-sheet therefore involve local regions in which each residue repeats stereochemically-desirable angles. You can predict the beta-strands but you cannot predict the partners. These procedures have led to the ramachandran plots (phi, psi maps)
