The crystal and molecular structure of the amino terminal tetrapeptide 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 tetrapeptide of alamethicin. A novel 310 helical conformation. In: Biochemical and Biophysical Research Communications, 79 (1). pp. 292-298.

PDF 2.pdf - Published Version Restricted to Registered users only Download (386kB) | Request a copy

Abstract

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

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	05 Feb 2010 06:58
Last Modified:	19 Sep 2010 05:49
URI:	http://eprints.iisc.ac.in/id/eprint/24156

Actions (login required)

View Item