By Alen Walton (Auth.)
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Peptide Pairs and Sequences In many synthetic pölypeptides and in all proteins, most of the peptide pairs do not contain equivalent peptides. It is, therefore, of considerable interest and importance to identify the modifications that hetero pairs introduce in conformational analysis. Very little work has been performed in this 56 2. Conformation area. That which has been carried through has concentrated on the L-proline residue because of its known conformation-directing properties. In the first reported work (1968) on Gly-L-Pro and L-Ala-L-Pro, Schimmel and Flory (26) concluded that the right-hand a-helix conformation is disallowed for an amino acid containing a ß carbon, which is followed by the prolyl residue.
Fig. 19. Drawings of the left-handed (a) and right-handed (b) a-helical forms of a polypeptide chain containing L-amino acids. [From B. W. Low and J. T. Edsall, in "Currents in Biochemical Research" (D. E. ), p. 398. ] * It is also of interest to note that the ß forms are degenerate, but different 2i helices, in the extended arrangement. Factors Controlling Conformation of Polypeptides 29 As we have seen, the number of possible intramolecularly hydrogen bonded helices is apparently very large. , less than 30°).
As a-helix formers, and it is highly likely that the steric maps for many peptide pairs will be very similar. The φ, φ angles for the various regular chain conformations have not been determined from atomic coordinates, but simply calculated, by means of the equations given in Chapter 3, from the observed n and h values obtained from the x-ray pattern. Direct determination of φ and φ has so far been possible only for certain globular proteins whose structures have been determined by single-crystal methods (see Chapter 13).