ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

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.

[img] PDF
2.pdf - Published Version
Restricted to Registered users only

Download (377Kb) | Request a copy
Official URL: http://www.sciencedirect.com/science?_ob=ArticleUR...

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
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.ernet.in/id/eprint/24156

Actions (login required)

View Item View Item