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

Author(s): J. Shobini, A. K. Mishra, Nagasuma Chandra

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 1 , 2001

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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.

Keywords: VPDLLADLLK, ornithine transcarbamylase, serine threonine phosphatase, Ni-Fe hydrogenase, thermostable B type DNA polymerase, cis -biphenyl-2,3-dihydrodiol-2,3-dehydrogenase

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Article Details

Year: 2001
Page: [49 - 55]
Pages: 7
DOI: 10.2174/0929866013409706

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