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

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

Volume: 8 Issue: 1

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

Affiliation:

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

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.

Cite this article as:

Shobini J., Mishra K. A. and Chandra Nagasuma, Cd Conformational And Modeling Studies Of A Synthetic Peptide Vpdlladllk In Different Media, Protein & Peptide Letters 2001; 8 (1) . https://dx.doi.org/10.2174/0929866013409706