Abstract
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.
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