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

研究成果: Contribution to journalArticle査読

4 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)798-804
ページ数7
ジャーナルJournal of Peptide Science
17
12
DOI
出版ステータス出版済み - 12 2011

All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 生化学
  • 分子医療
  • 分子生物学
  • 薬理学
  • 創薬
  • 有機化学

フィンガープリント

「NMR studies on thermal stability of α-helix conformation of melittin in pure ethanol and ethanol-water mixture solvents」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル