BMB 401 Lecture Notes - Lecture 3: Peptide Bond, Proline, Peptide
29 Nov 2016
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10: 1 = linear sequence of aa, 2 = a helices of b sheets. Not all polypeptides form these ordered structures and they are labelled structurally disordered. 100 degrees per residue) = 3. 6 res/turn: 5. 4 angstroms = how much it rises per helical turn = helical pitch. Lecture 3: helical rise = 5. 4 angstroms/turn / 3. 6 res/turn = 1. 5 angstrom/ residue, cylinder = helix in pictures. 12: a helix stabilized by h bonding, understand this!, a helix is 3. 6 residues/turn, twist = degrees/residue (360 degrees/turn / density, rise = angstrom/residue and get by dividing pitch/density. 13 b sheets: this is linear, not coiled. Extended conformation basically: can be parallel or antiparallel. 16: b sheet have inter-strand h bond. Parallel have diagonal h bonds and antiparallel have aligned h bonds. H bond between c=o and nh groups. Parallel have 12 in ring structure if you count. 25 26: understand, #10 gives chance you find it in that conformation.
