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

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

Document Type: Review Article


Publication date: February 1, 2001

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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