Table of Contents Author Guidelines Submit a Manuscript
E-Journal of Chemistry
Volume 7 (2010), Issue 3, Pages 1013-1017

Conformational Studies of ε- CBz- L- Lysine and L- Valine Block Copolypeptides

Ajay Kumar

Guru Tegh Bahadur Institute of Technology, G-8 Area, Rajouri Garden, New Delhi-110064, India

Received 22 October 2009; Accepted 15 December 2009

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Conformational studies of ε-CBz-L-lysine and L-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 are ε-CBz-L-lysine blocks. The conformation of the copolypeptides changes with increases in the chain length of ε- CBz-L- lysine blocks. When length of ε- CBZ- L- lysine blocks is 9, the block copolypeptide has exclusive beta sheet structure. With the increase in chain length of ε-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 of ε- CBz- L- lysine blocks, the beta sheet component disappears and block copolypeptides exhibits exclusive α -helix conformation.