title: Use of 19F NMR to probe protein structure and conformational changes.
abstract: 19F NMR has proven to be a powerful technique in the study of protein structure and dynamics because the 19F nucleus is easily incorporated at specific labeling sites, where it provides a relatively nonperturbing yet sensitive probe with no background signals. Recent applications of 19F 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 19F 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 19F 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 or line broadening of the 19F resonance by aqueous and membrane-bound paramagnetic probes, which may reveal the proximity of a 19F label to bulk solvent or a biological membrane. Finally, the effect of exchanging conformations on the 19F resonance can directly determine the kinetic parameters of the conformational transition.
authors.affiliation: Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215, USA.
authors.forename: M A
authors.initials: MA
authors.lastname: Danielson
authors.forename: J J
authors.initials: JJ
authors.lastname: Falke
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002633:Chemotaxis; D004926:Escherichia coli / Q000737:chemistry / Q000502:physiology; D029968:Escherichia coli Proteins; D005462:Fluorine Radioisotopes / Q000737:chemistry; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000502:physiology; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; D011487:Protein Conformation; D017459:Receptors, Amino Acid / Q000737:chemistry / Q000502:physiology; D012486:Salmonella typhimurium / Q000737:chemistry / Q000502:physiology; D012997:Solvents; D013329:Structure-Activity Relationship; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D005462:Fluorine Radioisotopes; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; D017459:Receptors, Amino Acid; D012997:Solvents; C031959:aspartic acid receptor; C000607606:cheY protein, E coli; C023550:galactose-binding protein; D007770:L-Lactate Dehydrogenase; D013762:Tetrahydrofolate Dehydrogenase