Affiliation:
1. Guru Tegh Bahadur Institute of Technology, G-8 Area, Rajouri Garden, New Delhi-110064, India
Abstract
Conformational studies ofε-CBz-L-lysine andL-valine block copoylpeptides using x- ray diffraction and CD spectra are described. The block copolypeptides contain valine block in the center and on both side of the valine areε-CBz-L-lysine blocks. The conformation of the copolypeptides changes with increases in the chain length ofε- CBz-L- lysine blocks. When length ofε- CBZ-L- lysine blocks is 9, the block copolypeptide has exclusive beta sheet structure. With the increase in chain length ofε-CBz-L-lysine blocks from 9 to 14, the block copolypeptide shows presence of both alpha helix and beta sheet components. With further increase in chain length ofε- CBz-L- lysine blocks, the beta sheet component disappears and block copolypeptides exhibits exclusive α -helix conformation.