NMR studies on thermal stability of α-helix conformation of melittin in pure ethanol and ethanol-water mixture solvents

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Abstract

Thermal stability of the α-helix conformation of melittin in pure ethanol and ethanol-water mixture solvents has been investigated by using NMR spectroscopy. With increase in water concentration of the mixture solvents (from 0wt% to ~71.5wt%) as well as temperature (from room temperature to 60°C), the intramolecular hydrogen bonds formed in melittin are destabilized and the α-helix is partially uncoiled. Further, the hydrogen bonds are found to be more thermally stable in pure ethanol than in pure methanol, suggesting that their stability is enhanced with increase in the size of the alkyl groups of alcohol molecules.

Original languageEnglish
Pages (from-to)798-804
Number of pages7
JournalJournal of Peptide Science
Volume17
Issue number12
DOIs
Publication statusPublished - Dec 2011

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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