Steady-state ATPase activity of E. coli MutS modulated by its dissociation from heteroduplex DNA

Biochemical and Biophysical Research Communications

Volumn 364, Issue 2, 2007, Pages 264-269

  Heo, Seong Dal ^a   Cho, Minseon ^a   Ku, Ja Kang ^a   Ban, Changill ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

Double end blocked heteroduplex; Gapped DNA; MutS; Spectrophotometric method; Steady state ATPase activity

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HETERODUPLEX; PROTEIN MUTS;

ARTICLE; BASE PAIRING; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; SPECTROPHOTOMETRY; STEADY STATE;

ADENOSINE TRIPHOSPHATASES; DNA, BACTERIAL; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; MUTS DNA MISMATCH-BINDING PROTEIN; NUCLEIC ACID HETERODUPLEXES;

ESCHERICHIA COLI;

EID: 35448967008     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.09.130     Document Type: Article

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