CHEM237 Chapter Notes - Chapter 6: Coiled Coil, Protein Folding, Oligomer
14 Nov 2016
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Secondary structure: local spatial arrangement of poly peptides - backbone of a poly peptide (not side chain con rmations) Peptide bond con rmation: no rotation around peptide bond (resonance/partial double bond character), usually in trans form (r groups of aa"s on opposite sides) c-n bond = C-c bond = , both are usually 180. Ramachandran diagram: due to steric hinderance, only certain values of and are allowed. Most areas are forbidden con rmations, pro restricts most, gly restricts least. 3. 6 residues per turn, rises 5. 4 a per turn. H bonds occur between nth and nth + Sheet: h bonding occurs between antiparallel pp chains, 2-22 pp"s w/ up to 15aa"s each. Strand length = # of aa"s x 3. 5 a/aa. Bends: occur at protein surface, 4aa"s allow for sharp turn. (usually pro and. Loop: large groups of different, well compacted structures often involved in protein function. Random coil: non repetitive structures w/ no clear pattern, resembles denatured proteins.
