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Aggregation studies in crystals of apolar helical peptides: Boc-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe

Karle, IL and Flippen-Anderson, JL and Uma, K and Balaram, Padmanabhan (1988) Aggregation studies in crystals of apolar helical peptides: Boc-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe. In: International Journal of Peptide & Protein Research Int J Pept Protein Res, 32 (6). pp. 536-543.

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Official URL: http://www.ncbi.nlm.nih.gov/pubmed/3246478

Abstract

In the crystal, the backbone of Boc-(Aib-Val-Ala-Leu)2-Aib-OMe adopts a helical form with four alpha-type hydrogen bonds in the middle, flanked by 3(10)-type hydrogen bonds at either end. The helical molecules stack in columns with head-to-tail hydrogen bonds, either directly between NH and CO, or bridged by solvent molecules. The packing of the helices is parallel, even in space group P2(1). Cell parameters are a = 9.837(2) A, b = 15.565(3) A, c = 20.087(5) A, beta = 96.42(2) degrees, dcalc = 1.091 g/cm3 for C46H83N9O12.1.5H2O.0.67CH3OH. There appears to be some hydration of the backbone in this apolar helix.

Item Type: Journal Article
Additional Information: Copy right of this article belongs toNational Center for Biotechnology Information.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 03 Jun 2010 08:54
Last Modified: 19 Sep 2010 06:00
URI: http://eprints.iisc.ernet.in/id/eprint/27231

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