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NMR studies on thermal stability of α ‐helix conformation of melittin in pure ethanol and ethanol–water mixture solvents
Author(s) -
Miura Yoshinori
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1405
Subject(s) - chemistry , melittin , ethanol , hydrogen bond , thermal stability , methanol , helix (gastropod) , alcohol , intramolecular force , molecule , organic chemistry , alkyl , circular dichroism , proton nmr , peptide , crystallography , biochemistry , ecology , snail , biology
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 0 wt% to ~71.5 wt%) 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. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.