Intermolecular (1)H[(19)F] NOEs in studies of fluoroalcohol-induced conformations of peptides and proteins.
J Magn Reson
; 152(2): 269-75, 2001 Oct.
Article
en En
| MEDLINE
| ID: mdl-11567580
ABSTRACT
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Trifluoroetanol
/
Espectroscopía de Resonancia Magnética
/
Proteínas
/
Muramidasa
Idioma:
En
Revista:
J Magn Reson
Asunto de la revista:
DIAGNOSTICO POR IMAGEM
Año:
2001
Tipo del documento:
Article
País de afiliación:
Estados Unidos