Title of article
Unusual structural transition of antimicrobial VP1 peptide
Author/Authors
Ganesh Shanmugam، نويسنده , , Nsoki Phambu، نويسنده , , Prasad L. Polavarapu، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2011
Pages
5
From page
104
To page
108
Abstract
VP1 peptide, an active domain of m-calpain enzyme with antimicrobial activity is found to undergo an unusual conformational transition in trifluoroethanol (TFE) solvent. The nature of, and time dependent variations in, circular dichroism associated with the amide I vibrations, suggest that VP1 undergoes self-aggregation forming anti-parallel β-sheet structure in TFE. Transmission electron micrograph (TEM) images revealed that β-sheet aggregates formed by VP1 possess fibril-like assemblies.
Keywords
Vibrational circular dichroism , VP1 peptide , Antimicrobial , Electronic circular dichroism , ?-Sheet , fibril
Journal title
Biophysical Chemistry
Serial Year
2011
Journal title
Biophysical Chemistry
Record number
1120448
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