Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM045990-04
Application #
2183591
Study Section
Special Emphasis Panel (ZRG3-BBCA (01))
Project Start
1991-05-01
Project End
2000-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
4
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
Vanderbilt University Medical Center
Department
Physiology
Type
Schools of Medicine
DUNS #
004413456
City
Nashville
State
TN
Country
United States
Zip Code
37212

  Publications

Whitesell, Richard R; Ardehali, Hossein; Beechem, Joseph M et al. (2005) Compartmentalization of transport and phosphorylation of glucose in a hepatoma cell line. Biochem J 386:245-53
Allan, B W; Reich, N O; Beechem, J M (1999) Measurement of the absolute temporal coupling between DNA binding and base flipping. Biochemistry 38:5308-14
Bilsel, O; Yang, L; Zitzewitz, J A et al. (1999) Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry 38:4177-87
Beechem, J M; Otto, M R; Bloom, L B et al. (1998) Exonuclease-polymerase active site partitioning of primer-template DNA strands and equilibrium Mg2+ binding properties of bacteriophage T4 DNA polymerase. Biochemistry 37:10144-55
Meagher, J L; Beechem, J M; Olson, S T et al. (1998) Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding. J Biol Chem 273:23283-9
Otto, M R; Bloom, L B; Goodman, M F et al. (1998) Stopped-flow fluorescence study of precatalytic primer strand base-unstacking transitions in the exonuclease cleft of bacteriophage T4 DNA polymerase. Biochemistry 37:10156-63
Lanzo, C A; Beechem, J M; Talley, J et al. (1998) Investigation of the binding of isoform-selective inhibitors to prostaglandin endoperoxide synthases using fluorescence spectroscopy. Biochemistry 37:217-26
Beechem, J M (1997) Picosecond fluorescence decay curves collected on millisecond time scale: direct measurement of hydrodynamic radii, local/global mobility, and intramolecular distances during protein-folding reactions. Methods Enzymol 278:24-49
Lillo, M P; Beechem, J M; Szpikowska, B K et al. (1997) Design and characterization of a multisite fluorescence energy-transfer system for protein folding studies: a steady-state and time-resolved study of yeast phosphoglycerate kinase. Biochemistry 36:11261-72
Lillo, M P; Szpikowska, B K; Mas, M T et al. (1997) Real-time measurement of multiple intramolecular distances during protein folding reactions: a multisite stopped-flow fluorescence energy-transfer study of yeast phosphoglycerate kinase. Biochemistry 36:11273-81

Showing the most recent 10 out of 17 publications