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

Authors: Shobini J.; Mishra A.K.; Chandra N.

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 49-55(7)

Publisher: Bentham Science Publishers

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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.

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

Language: English

Document Type: Review article

DOI: 10.2174/0929866013409706

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