Continued support is requested for a regional high-resolution NMR facility for the study of biological systems housed in the Department of Chemistry, Purdue University. The Facility is designed to handle the severe problems of resolution and sensitivity encountered with biological macromolecules. The research proposals submitted by users of the Facility cover several general areas: structure and function of proteins, nucleic acids, membranes, and natural products; active sites of enzymes; modes of action of drugs; and physiological levels of metabolites in living cells and organisms. The Facility is based on two multinuclear spectrometers, 11.1 T narrow-bore and 4.7 T wide-bore. The efficiencies of these will be increased by adding computer controlled field shims and an off-line data processing station, which will be used for training and core research. The versatility of the Facility will be expanded by the addition of broad-banded probes and instrumentation for saturation transfer, laser CIDNP, and selective relaxation experiments. Although the primary function of the Facility is to provide an effective research tool to its users, part of the efforts of its staff are directed toward technological development in the areas of probe sensitivity, efficient multinuclear operation, variable temperature operation, custom probes for specialized experiments, and effective processing, storage, and presentation of spectra. The Facility is administered by an Advisory Committee consisting of the Principal Investigator, representative users, and nationally recognized experts in the field. Service time on the spectrometers is apportioned according to the scientific merit of the research as determined by the Advisory Committee.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001077-08
Application #
3103738
Study Section
(SSS)
Project Start
1977-08-01
Project End
1986-07-31
Budget Start
1985-03-01
Budget End
1986-02-28
Support Year
8
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Purdue University
Department
Type
Schools of Arts and Sciences
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907
Ray, B D; Chau, M H; Fife, W K et al. (1996) Conformation of manganese(II)-nucleotide complexes bound to rabbit muscle creatine kinase: 13C NMR measurements using [2-13C]ATP and [2-13C]ADP. Biochemistry 35:7239-46
Ray Jr, W J; Post, C B; Puvathingal, J M (1993) Reaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited. Biochemistry 32:38-47
Ray Jr, W J; Post, C B; Liu, Y et al. (1993) Structural changes at the metal ion binding site during the phosphoglucomutase reaction. Biochemistry 32:48-57
Nikonowicz, E P; Meadows, R P; Fagan, P et al. (1991) NMR structural refinement of a tandem G.A mismatched decamer d(CCAAGATTGG)2 via the hybrid matrix procedure. Biochemistry 30:1323-34
Zhang, Z Y; VanEtten, R L (1991) Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. J Biol Chem 266:1516-25
Nikonowicz, E P; Gorenstein, D G (1990) Two-dimensional 1H and 31P NMR spectra and restrained molecular dynamics structure of a mismatched GA decamer oligodeoxyribonucleotide duplex. Biochemistry 29:8845-58
Gan, L X; Whistler, R L (1990) Formylation of primary hydroxyl groups in sugars. Carbohydr Res 206:65-9
Powers, R; Gorenstein, D G (1990) Two-dimensional 1H and 31P NMR spectra and restrained molecular dynamics structure of a covalent CPI-CDPI2-oligodeoxyribonucleotide decamer complex. Biochemistry 29:9994-10008
Alkofahi, A; Rupprecht, J K; Liu, Y M et al. (1990) Gigantecin: a novel antimitotic and cytotoxic acetogenin, with nonadjacent tetrahydrofuran rings, from Goniothalamus giganteus (Annonaceae). Experientia 46:539-41
Ray Jr, W J; Post, C B (1990) The oxyvanadium constellation in transition-state-analogue complexes of phosphoglucomutase and ribonuclease. Structural deductions from electron-transfer spectra. Biochemistry 29:2779-89

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