Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer

Nucleic Acids Research

Volumn 37, Issue 6, 2009, Pages 1962-1972

  Wagner, Koen ^a   Moolenaar, Geri ^a   van Noort, John ^b   Goosen, Nora ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

^b LEIDEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DNA BINDING PROTEIN; PROTEIN UVRA; UNCLASSIFIED DRUG; DNA; ESCHERICHIA COLI PROTEIN; UVRA PROTEIN, E COLI;

ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING AFFINITY; CONTROLLED STUDY; DIMERIZATION; DNA DAMAGE; DNA FLANKING REGION; DNA FRAGMENTATION; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; CHEMISTRY; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; DIMERIZATION; DNA; DNA DAMAGE; DNA-BINDING PROTEINS; ESCHERICHIA COLI PROTEINS; MICROSCOPY, ATOMIC FORCE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY;

EID: 64549144120     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp071     Document Type: Article

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