Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR

研究成果: Contribution to journalArticle査読

4 被引用数 (Scopus)

抄録

Temperature dependence of the α-helix conformation of bee venom melittin in methanol-water mixed solvents has been examined by NMR, in order to elucidate conformation stability and a phase diagram. At high methanol concentration of 100 - ca. 80 wt.%, melittin forms a full α-helix conformation in the temperature range from 25 °C to 60 °C. At intermediate methanol concentration of ca. 80 - ca. 25 wt.%, it undergoes a thermal transformation from a full α-helix to a partial α-helix. In solutions of low methanol concentrations of ca. 25 - 0 wt.%, partial α-helix monomers and their selfaggregated conformers coexist at low temperatures, and the relative number of the monomers increases with increase in temperature. The monomers turn to a random coil state at high temperatures only below ca. 10 wt. % methanol concentrations. The thermal transitions are discussed from the viewpoint of stability of intra-molecular hydrogen bonds and intermolecular hydrophobic interactions.

本文言語英語
ページ(範囲)318-326
ページ数9
ジャーナルProtein and Peptide Letters
18
3
DOI
出版ステータス出版済み - 3 2011

All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 生化学

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