A quantitative analysis of the effect of nucleotides and the M Domain on the Association Equilibrium of ClpB

Biochemistry

Volumn 50, Issue 12, 2011, Pages 1991-2003

  Del Castillo, Urko ^a   Alfonso, Carlos ^b   Acebrón, Sergio P ^a,c   Martos, Ariadna ^b   Moro, Fernando ^a   Rivas, Germán ^b   Muga, Arturo ^a  

^a UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^b CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; ASSOCIATION EQUILIBRIA; BIOLOGICAL IMPLICATIONS; BOUND STATE; CHAPERONE ACTIVITY; CIRCULAR DICHROISM; CONFORMATIONAL CHANGE; DELETION MUTANTS; DENATURED PROTEINS; EXPERIMENTAL CONDITIONS; HEXAMERS; HIGHER ORDER; INTERSUBUNIT INTERACTION; MOLECULAR CHAPERONES; NUCLEOTIDE EXCHANGE; PROTEIN PARTICLES; PROTEIN SECONDARY STRUCTURE; QUANTITATIVE ANALYSIS; STATIC LIGHT SCATTERING; WILD TYPES;

CENTRIFUGATION; CHEMICAL ANALYSIS; DICHROISM; NUCLEOTIDES; OLIGOMERIZATION; OLIGOMERS;

PROTEINS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; DODECAMER; HEXAMER; M PROTEIN; MONOMER; NUCLEOTIDE; OLIGOMER; POLYMER; PROTEIN; PROTEIN CLPB; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CHEMICAL ANALYSIS; CIRCULAR DICHROISM; COMPOSITION GRADIENT STATIC LIGHT SCATTERING; CONTROLLED STUDY; ENZYME ACTIVITY; EQUILIBRIUM CONSTANT; GENE DELETION; LIGHT SCATTERING; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; ULTRACENTRIFUGATION; WILD TYPE;

ADENOSINE TRIPHOSPHATE; HEAT-SHOCK PROTEINS; HYDRODYNAMICS; MODELS, MOLECULAR; NUCLEOTIDES; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; THERMODYNAMICS;

EID: 79952906659     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101670s     Document Type: Article

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