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首页> 外文期刊>Journal of peptide science: An official publication of the European Peptide Society >NMR studies on thermal stability of α-helix conformation of melittin in pure ethanol and ethanol-water mixture solvents
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NMR studies on thermal stability of α-helix conformation of melittin in pure ethanol and ethanol-water mixture solvents

机译:NMR研究蜂毒肽在纯乙醇和乙醇-水混合溶剂中的α-螺旋构型的热稳定性

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摘要

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.
机译:蜂毒肽在纯乙醇和乙醇-水混合溶剂中的α-螺旋构型的热稳定性已通过NMR光谱法进行了研究。随着混合溶剂的水浓度(从0wt%到〜71.5wt%)以及温度(从室温到60°C)的增加,在蜂毒蛋白中形成的分子内氢键不稳定,α-螺旋部分解开。此外,发现氢键在纯乙醇中比在纯甲醇中更热稳定,表明它们的稳定性随着醇分子烷基大小的增加而增强。

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