Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32GM013324-02
Application #
3044424
Study Section
Special Emphasis Panel (BI)
Project Start
1990-11-01
Project End
Budget Start
1990-11-01
Budget End
1991-10-31
Support Year
2
Fiscal Year
1990
Total Cost
Indirect Cost
Name
Johns Hopkins University
Department
Type
Schools of Medicine
DUNS #
045911138
City
Baltimore
State
MD
Country
United States
Zip Code
21218
Weber, D J; Libson, A M; Gittis, A G et al. (1994) NMR docking of a substrate into the X-ray structure of the Asp-21-->Glu mutant of staphylococcal nuclease. Biochemistry 33:8017-28
Weber, D J; Serpersu, E H; Gittis, A G et al. (1993) NMR docking of the competitive inhibitor thymidine 3',5'-diphosphate into the X-ray structure of staphylococcal nuclease. Proteins 17:20-35
Chuang, W J; Weber, D J; Gittis, A G et al. (1993) Mutational tests of the NMR-docked structure of the staphylococcal nuclease-metal-3',5'-pdTp complex. Proteins 17:36-48
Mildvan, A S; Weber, D J; Kuliopulos, A (1992) Quantitative interpretations of double mutations of enzymes. Arch Biochem Biophys 294:327-40
Weber, D J; Bhatnagar, S K; Bullions, L C et al. (1992) NMR and isotopic exchange studies of the site of bond cleavage in the MutT reaction. J Biol Chem 267:16939-42
Weber, D J; Gittis, A G; Mullen, G P et al. (1992) NMR docking of a substrate into the X-ray structure of staphylococcal nuclease. Proteins 13:275-87
Weber, D J; Mullen, G P; Mildvan, A S (1991) Conformation of an enzyme-bound substrate of staphylococcal nuclease as determined by NMR. Biochemistry 30:7425-37
Weber, D J; Meeker, A K; Mildvan, A S (1991) Interactions of the acid and base catalysts on staphylococcal nuclease as studied in a double mutant. Biochemistry 30:6103-14
Weber, D J; Serpersu, E H; Shortle, D et al. (1990) Diverse interactions between the individual mutations in a double mutant at the active site of staphylococcal nuclease. Biochemistry 29:8632-42