The crystal and molecular structure of the amino terminal tetra-peptide of alamethicin. A novel 310 helical conformation

Shamala, N and Nagaraj, R and Balaram, P (1977) The crystal and molecular structure of the amino terminal tetra-peptide of alamethicin. A novel 310 helical conformation. In: Biochemical and Biophysical Research Communications, 79 (1). pp. 292-298.

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Abstract

The molecular Structure of N-benzyloxycarbonyl-a-aminoisobutyryl-prolyl-a-aminoisobutyryl-alanyl methyl ester (z-Aib-Pro-Aib-Ala-OMe), the amino terminal tetrapeptide of alamethicin is reported. The molecule contains two consecutive b- turns with Aib-Pro and Pro-Aib at the corners, forming an incipient 310 helix. This constitutes the first example of X2-Pro3 b-turn in the crystal structure of a small peptide.

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Academic Press
Additional Information:	Copyright for this article belongs to Academic Press
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	26 Jul 2004
Last Modified:	19 Sep 2010 04:14
URI:	http://eprints.iisc.ac.in/id/eprint/1173

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