The Escherichia coli primosomal dnat protein exists in solution as a monomer-trimer equilibrium system

Biochemistry

Volumn 52, Issue 11, 2013, Pages 1845-1857

  Szymanski, Michal R ^a   Jezewska, Maria J ^a   Bujalowski, Wlodzimierz ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; C-TERMINAL REGIONS; CONFORMATIONAL TRANSITIONS; EQUILIBRIUM SYSTEMS; FLUORESCENCE ANISOTROPY; HIGHLY COOPERATIVES; INTERACTING SITES; N-TERMINAL DOMAINS;

CENTRIFUGATION; ESCHERICHIA COLI; MONOMERS; OLIGOMERIZATION; PROTEINS;

DIMERS;

ESCHERICHIA COLI DNAT PROTEIN; ESCHERICHIA COLI PROTEIN; MONOMER; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; COMPUTER SIMULATION; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DIMERIZATION; ESCHERICHIA COLI; HYDRATION; HYDRODYNAMICS; MOLECULAR WEIGHT; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; SEDIMENTATION; SEDIMENTATION RATE; STEADY STATE; STOICHIOMETRY; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; ULTRACENTRIFUGATION;

ESCHERICHIA COLI;

EID: 84875472588     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301568w     Document Type: Article

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