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

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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.

元の言語英語
ページ(範囲)798-804
ページ数7
ジャーナルJournal of Peptide Science
17
発行部数12
DOI
出版物ステータス出版済み - 12 1 2011

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All Science Journal Classification (ASJC) codes

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

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