By Alen Walton (Auth.)
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14) of 0°-30°. The possible sites of hydrogen bonding in a single polypeptide chain (backbone) were suggested in 1950 by Bragg et al. (3) and are shown schematically in Fig. 15. Such intramolecular hydrogen bonds would cause the chain to twist into a helix. Note that two different hydrogen-bonded ring systems are apparently possible (Figs. 17), containing 3n' + 4 (type A) and 3«' + 5 (type B) atoms, respectively. Although we now know Factors Controlling Conformation of Polypeptides x 27 (NH-CHR-CO)„ Fig.
G, J. O. Hirschfelder and J. W. Linnett, / . Chem. Phys. 18, 130 (1950); P. DeSantis, E. Giglio, A. M. Liquori, and A. Ripaimonti, /. Polym. Sei. AI, 1383 (1963). H, A. J. Hopfinger and A. G. Walton, /. Macromol. Sei. Phys. B3, 171 (1969). I, R. A. Scott and H. A. Scheraga, /. Chem. Phys. 42,2209 (1965). 28 shows the results of nine different proposed functions for the H · · · H atom interaction. The derivation of potential energy curves relating the interaction energy of two atoms to the distance between their centers involves the assumption that the energy at a given distance is essentially independent of orientation of the atoms and the nature and strength of any bonds between the atoms.
22. Chain arrangement in the parallel β sheet. 31 Factors Controlling Conformation of Polypeptides Fig. 23. Schematic three-dimensional representation of a molecular chain in the ß conformation showing the "pleated sheet" effect. [From G. M. Barrow "Physical Chemistry" McGraw Hill, New York (1966) p. 9 a Rational helices quoted. * Positive values for right-hand, negative for left-hand helices. 32 2. , 185) helices. , backbone rotation angles and dihedral angles, must also bear some definable relation to the characterization of helices.
Biopolymers by Alen Walton (Auth.)