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

Journal of Peptide Science

Volumn 17, Issue 12, 2011, Pages 798-804

  Miura, Yoshinori ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

helix; Ethanol; Hydrogen bond; Hydrophobic interaction; Melittin; NMR; Thermal stability

Indexed keywords

ALCOHOL; ALKYL GROUP; MELITTIN; SOLVENT; WATER;

ALPHA HELIX; ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATION; CROSS LINKING; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STRUCTURE; ROOM TEMPERATURE; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

AMINO ACID SEQUENCE; ETHANOL; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MELITTEN; MOLECULAR SEQUENCE DATA; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; TEMPERATURE; WATER;

EID: 81155123195     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1405     Document Type: Article

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