By G. N. Ramachandran
Read Online or Download Conformation of Biopolymers. Papers Read at an International Symposium Held at the University of Madras, 18–21 January 1967 PDF
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K. (1959). D. thesis, Massachusetts Institute of Technology. , Silman, H. I. & Berger, A. (1964). In "The Proteins", ed. by H. Neurath, Vol. 2, p. 405. New York: Academic Press. Kendrew, J. C. (1962). Brookhaven Symp. quant. Biol. 15, 216. , Baudras, A. & Blout, E. R. (1958). / . Am. chem. Soc. 80, 6191. , Masson, F. & Vincent, J. M. (1961). J. molec. Biol. 3, 566. , Masson, F. & Vincent, J. M. (1962). In "Polyamino Acids, Polypeptides and Proteins", ed. by M. A. Stahmann, p. 121. Madison: University of Wisconsin Press.
By G. Stainsby, p. 25. London: Pergamon Press. Carver, J. , Shechter, E. & Blout, E. R. (1966a). / . Am. chem. Soc. 88, 2550. Carver, J. , Shechter, E. & Blout, E. R. (19660). / . Am. chem. Soc. 88, 2562. Cowan, P. , McGavin, S. & North, A. C. T. (1955). Nature, Lond. 176, 1062. Downie, A. R. & Randall, A. (1962). In "Collagen", ed. by N. Ramanathan, p. 209. New York : Interscience. , Berger, A. & Katchalski, E. (1965). In "Structure and Function of Connective and Skeletal Tissue", ed. by S. F.
The 9-3 Â c-axis corresponds to one tripeptide unit and one turn of the poly peptide helix. The 4-9 Â 6-axis is related to the width of the chains and to the mode of interchain hydrogen bonding. It therefore seems likely that the conformation of the chains and the hydrogen bonding between them is unaffected by the solvent. However, the sheets of polypeptide chains become slightly staggered and the distance between them increases providing space for the incorporation of formic acid, possibly in the vicinity of the unbonded carbonyl groups.