LexA repressor forms stable dimers in solution. The role of specific DNA in tightening protein-protein interactions

Journal of Biological Chemistry

Volumn 275, Issue 7, 2000, Pages 4708-4712

  Mohana Borges, Ronaldo ^a   Pacheco, Ana B F ^a   Sousa, Francisco J R ^a   Foguel, Debora ^a   Almeida, Darcy F ^a   Silva, Jerson L ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DNA; MONOMER; REPRESSOR PROTEIN; UREA;

ARTICLE; CONCENTRATION (PARAMETERS); DISSOCIATION CONSTANT; DNA BINDING; DNA REPAIR; DNA SEQUENCE; FLUORESCENCE; HYDROSTATIC PRESSURE; MOLECULAR RECOGNITION; POLARIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DNA INTERACTION; PROTEIN PROTEIN INTERACTION;

BACTERIAL PROTEINS; BASE SEQUENCE; CHROMATOGRAPHY, GEL; DIMERIZATION; DNA; ELECTROPHORESIS, POLYACRYLAMIDE GEL; SERINE ENDOPEPTIDASES; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 0034681384     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.7.4708     Document Type: Article

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