Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI030725-05
Application #
2065840
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1991-02-01
Project End
1997-01-31
Budget Start
1995-02-01
Budget End
1997-01-31
Support Year
5
Fiscal Year
1995
Total Cost
Indirect Cost
Name
University of California Berkeley
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704
Yeh, J I; Biemann, H P; Prive, G G et al. (1996) High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor. J Mol Biol 262:186-201
Wolf, A; Shaw, E W; Oh, B H et al. (1995) Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form. J Biol Chem 270:16097-106
Oh, B H; Ames, G F; Kim, S H (1994) Structural basis for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein. J Biol Chem 269:26323-30
Jamieson, A C; Kim, S H; Wells, J A (1994) In vitro selection of zinc fingers with altered DNA-binding specificity. Biochemistry 33:5689-95
Kim, S H (1994) ""Frozen"" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors. Protein Sci 3:159-65
Oh, B H; Kang, C H; De Bondt, H et al. (1994) The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. J Biol Chem 269:4135-43
Oh, B H; Pandit, J; Kang, C H et al. (1993) Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J Biol Chem 268:11348-55
Yeh, J I; Biemann, H P; Pandit, J et al. (1993) The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem 268:9787-92
Scott, W G; Milligan, D L; Milburn, M V et al. (1993) Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium. J Mol Biol 232:555-73
Kim, S H; Prive, G G; Yeh, J et al. (1992) A model for transmembrane signaling in a bacterial chemotaxis receptor. Cold Spring Harb Symp Quant Biol 57:17-24

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