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Cd Conformational And Modeling Studies Of A Synthetic Peptide Vpdlladllk In Different Media

Shobini, J and Mishra, AK and Chandra, N (2001) Cd Conformational And Modeling Studies Of A Synthetic Peptide Vpdlladllk In Different Media. In: Protein & Peptide Letters, 8 (1). pp. 49-55.

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Abstract

CD spectral studies of VPDLLADLK, a synthetic peptide shows that it undergoes a conformational transition from an unordered structure to a more ordered structure from a polar to a non-polar homogeneous medium. In microheterogeneous media like SDS, CTAB micelles and DMPC lipid bilayer, the peptide exhibits a more stable alpha- helical structure. The helical conformation is stabilized in DMPC lipid bilayer. Homology modeling gives the picture of alpha- helix, where the middle six residues LLADLL form the turns of the helix.

Item Type: Journal Article
Additional Information: Copyright belongs to this article belongs to Bentham Science Publishers
Keywords: VPDLLADLLK;ornithine transcarbamylase;serine threonine phosphatase;Ni-Fe hydrogenase;thermostable B type DNA polymerase;cis -biphenyl-2,3-dihydrodiol-2,3-dehydrogenase
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited: 17 Dec 2008 14:11
Last Modified: 08 Dec 2009 09:34
URI: http://eprints.iisc.ernet.in/id/eprint/16633

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