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- W1996060883 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." @default.
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- W1996060883 date "2011-05-01" @default.
- W1996060883 modified "2023-09-27" @default.
- W1996060883 title "Unusual structural transition of antimicrobial VP1 peptide" @default.
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- W1996060883 doi "https://doi.org/10.1016/j.bpc.2011.03.005" @default.
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