C-H center dot center dot center dot O hydrogen bond mediated chain reversal in a peptide containing a \gamma-amino acid residue, determined directly from powder X-ray diffraction data

Cheung, EY and McCabe, EE and Harris, KDM and Johnston, RL and Tedesco, E and Raja, KMP and Balaram, P (2002) C-H center dot center dot center dot O hydrogen bond mediated chain reversal in a peptide containing a \gamma-amino acid residue, determined directly from powder X-ray diffraction data. In: Wiley-Vch Verlag GmbH, 41 (3). pp. 494-496.

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Abstract

The finding that peptides containing -amino acid residues give rise to folding patterns hitherto unobserved in -amino acid peptides[1] has stimulated considerable interest in the conformational properties of peptides built from , , and residues,[2] as the introduction of additional methylene (CH2) units into peptide chains provides further degrees of conformational freedom. Studies of the influence of introducing-amino acids into regular polypeptide structures derived from residues have demonstrated that extra methylene groups can be inserted into helical backbones and into the strand and turn segments of hairpins.[3] In regard to the influence of CH2 group insertion into the i2 position of isolated peptide turns, we are investigating the conformational properties of a series of model sequences Piv-Pro-Xxx- NHMe (defined in Scheme 1 and reference [4]).

Item Type:	Journal Article
Publication:	Wiley-Vch Verlag GmbH
Publisher:	Wiley-Vch Verlag GmbH
Additional Information:	Copyright of this article belongs to Wiley-Vch Verlag GmbH.
Keywords:	Crystal-Structure Determination;Genetic Algorithm;Secondary Structure;Beta-Peptides;Design;Conformations;Hexapeptide; Patterns;Proteins;Helices
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	09 Mar 2009 11:48
Last Modified:	19 Sep 2010 05:00
URI:	http://eprints.iisc.ac.in/id/eprint/18238

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