Intermolecular (1)H[(19)F] NOEs in studies of fluoroalcohol-induced conformations of peptides and proteins.
Mixtures of fluorinated alcohols and water can selectively stabilize certain secondary structures of peptides and proteins. Such mixtures may also be of use in solubilizing hydrophobic or membrane-bound proteins. We show that intermolecular dipolar interactions between the fluorine nuclei of such solvents and the protons of a dissolved protein lead to readily detected (1)H[(19)F] nuclear Overhauser effects. These NOEs can potentially provide information about solvent exposure of particular groups as well as indicate the formation of long-lived fluoroalcohol-solute complexes. Results obtained with HEW lysozyme in solutions containing trifluoroethanol illustrate these possibilities.
Martinez
D
D
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.
Gerig
J T
JT
D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012815:Signal Processing, Computer-Assisted; D014270:Trifluoroethanol / Q000737:chemistry*
D010455:Peptides; D011506:Proteins; D014270:Trifluoroethanol; D009113:Muramidase