Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM018277-19
Application #
3269214
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1979-05-01
Project End
1989-07-31
Budget Start
1989-05-01
Budget End
1989-07-31
Support Year
19
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Brandeis University
Department
Type
Schools of Arts and Sciences
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
02454
Seedorff, Jennifer; Schleif, Robert (2011) Active role of the interdomain linker of AraC. J Bacteriol 193:5737-46
Berrondo, Monica; Gray, Jeffrey J; Schleif, Robert (2010) Computational predictions of the mutant behavior of AraC. J Mol Biol 398:462-70
Seedorff, Jennifer E; Rodgers, Michael E; Schleif, Robert (2009) Opposite allosteric mechanisms in TetR and CAP. Protein Sci 18:775-81
Rodgers, Michael E; Schleif, Robert (2009) Solution structure of the DNA binding domain of AraC protein. Proteins 77:202-8
Rodgers, Michael E; Holder, Nakisha D; Dirla, Stephanie et al. (2009) Functional modes of the regulatory arm of AraC. Proteins 74:81-91
Dirla, Stephanie; Chien, John Yeh-Heng; Schleif, Robert (2009) Constitutive mutations in the Escherichia coli AraC protein. J Bacteriol 191:2668-74
Frato, Katherine E; Schleif, Robert F (2009) A DNA-assisted binding assay for weak protein-protein interactions. J Mol Biol 394:805-14
Hargreaves, Victoria V; Schleif, Robert F (2008) The salt dependence of the interferon regulatory factor 1 DNA binding domain binding to DNA reveals ions are localized around protein and DNA. Biochemistry 47:4119-28