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Titolo:
USE OF F-19 NMR TO PROBE PROTEIN-STRUCTURE AND CONFORMATIONAL-CHANGES
Autore:
DANIELSON MA; FALKE JJ;
Indirizzi:
UNIV COLORADO,DEPT CHEM & BIOCHEM BOULDER CO 80309
Titolo Testata:
Annual review of biophysics and biomolecular structure
, volume: 25, anno: 1996,
pagine: 163 - 195
SICI:
1056-8700(1996)25:<163:UOFNTP>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; D-LACTATE DEHYDROGENASE; GALACTOSE CHEMOSENSORY RECEPTOR; DIRECTED CROSS-LINKING; ALL-TRANS-RETINOL; ESCHERICHIA-COLI; BINDING-PROTEIN; BACTERIAL CHEMOTAXIS; CHEMICAL-SHIFTS; SIGNAL TRANSDUCTION;
Keywords:
FLUORINE; PARAMAGNETIC BROADENING; SPIN-LABEL; DYNAMICS; X-RAY CRYSTALLOGRAPHY;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
100
Recensione:
Indirizzi per estratti:
Citazione:
M.A. Danielson e J.J. Falke, "USE OF F-19 NMR TO PROBE PROTEIN-STRUCTURE AND CONFORMATIONAL-CHANGES", Annual review of biophysics and biomolecular structure, 25, 1996, pp. 163-195

Abstract

F-19 NMR has proven to be a powerful technique in the study of protein structure and dynamics because the F-19 nucleus is easily incorporated at specific labeling sites, where it provides a relatively nonperturbing yet sensitive probe with no background signals. Recent applications of F-19 NMR in mapping out structural and functional features of proteins, including the galactose-binding protein, the transmembrane aspartate receptor, the CheY protein, dihydrofolate reductase, elongation factor-Tu, and D-lactose dehydrogenase, illustrate the utility of F-19 NMR in the analysis of protein conformational states even in molecules too large or unstable for full NMR structure determination. These studies rely on the fact that the chemical shift of F-19 is extremely sensitive to changes in the local conformational environment, including van der Waals packing interactions and local electrostatic fields. Additional information is provided by solvent-induced isotope shifts orline broadening of the F-19 resonance by aqueous and membrane-bound paramagnetic probes, which may reveal the proximity of a F-19 label to bulk solvent or a biological membrane. Finally, the effect of exchanging conformations on the F-19 resonance can directly determine the kinetic parameters of the conformational transition.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:42:45