Interactions of 2,2,2-trifluoroethanol with melittin

2009 John Wiley & Sons, Ltd.

Bibliographische Detailangaben
Veröffentlicht in:Magnetic resonance in chemistry : MRC. - 1985. - 47(2009), 11 vom: 01. Nov., Seite 925-31
1. Verfasser: Neuman, Robert C Jr (VerfasserIn)
Weitere Verfasser: Gerig, John T
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Magnetic resonance in chemistry : MRC
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Melitten 20449-79-0 Trifluoroethanol 75-89-8
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520 |a Melittin dissolved in 42% trifluoroethanol-water at pH 2 has been shown to be alpha-helical between residues 6 and 12 and between residues 13 and 25, with the two helical regions separated by a bend at the Leu13 residue. The inter-helix angle was found to be 154 +/- 3 degrees at 0 degrees C and 135 +/- 3 degrees at 25 degrees C. The dominant conformation of the peptide is thus similar to those observed by previous workers for the peptide in a variety of media. At 25 degrees C, intermolecular nuclear Overhauser effects arising from nuclear spin dipole-dipole interactions between melittin hydrogens and fluorines of the solvent are essentially those expected for a system that is homogeneous as regards concentration and translational diffusion of the peptide and fluoroalcohol components. However, at 0 degrees C, peptide-trifluoroethanol cross-relaxation terms are negative, a result consistent with the conclusion that fluoroalcohol molecules associate with the peptide for times (approximately 1 ns) that are long compared to the time of a typical peptide-fluoroalcohol diffusive encounter (approximately 0.2 ns). Such interactions may be responsible for the reduction of the translational diffusion coefficient of trifluoroethanol produced by dissolved peptides 
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