Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM039343-08
Application #
2179767
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1989-07-01
Project End
1998-08-31
Budget Start
1996-09-01
Budget End
1997-08-31
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Washington University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
062761671
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Darling, P J; Holt, J M; Ackers, G K (2000) Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations. Biochemistry 39:11500-7
Darling, P J; Holt, J M; Ackers, G K (2000) Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding II: cooperative interactions of cro dimers. J Mol Biol 302:625-38
Merabet, E K; Burz, D S; Ackers, G K (1998) Thermal melting properties of C-terminal domain mutants of bacteriophage lambda cI repressor. Methods Enzymol 295:450-67
Pray, T R; Burz, D S; Ackers, G K (1998) Cooperative non-specific DNA binding by octamerizing lambda cI repressors: a site-specific thermodynamic analysis. J Mol Biol 282:947-58
Bain, D L; Ackers, G K (1998) A quantitative cryogenic gel-shift technique for analysis of protein-DNA binding. Anal Biochem 258:240-5
Burz, D S; Ackers, G K (1996) Cooperativity mutants of bacteriophage lambda cI repressor: temperature dependence of self-assembly. Biochemistry 35:3341-50
Merabet, E; Ackers, G K (1995) Calorimetric analysis of lambda cI repressor binding to DNA operator sites. Biochemistry 34:8554-63
Bain, D L; Ackers, G K (1994) Self-association and DNA binding of lambda cI repressor N-terminal domains reveal linkage between sequence-specific binding and the C-terminal cooperativity domain. Biochemistry 33:14679-89
Burz, D S; Beckett, D; Benson, N et al. (1994) Self-assembly of bacteriophage lambda cI repressor: effects of single-site mutations on the monomer-dimer equilibrium. Biochemistry 33:8399-405
Burz, D S; Ackers, G K (1994) Single-site mutations in the C-terminal domain of bacteriophage lambda cI repressor alter cooperative interactions between dimers adjacently bound to OR. Biochemistry 33:8406-16

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