Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range

Biochemistry

Volumn 45, Issue 39, 2006, Pages 12090-12099

  Connaghan Jones, Keith D ^a   Heneghan, Aaron F ^a   Miura, Michael T ^a   Bain, David L ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC MECHANISMS; ASSEMBLY REACTIONS; CONCENTRATION-DEPENDENT; DRIVING FORCES; FOLDED CONFORMATION; GLOBAL ANALYSIS; HYDRODYNAMIC ANALYSIS; ISOFORMS; LIMITED PROTEOLYSIS; MICROMOLAR CONCENTRATION; MICROMOLAR RANGE; MONOMER SPECIES; N-TERMINALS; PROGESTERONE RECEPTOR; SEDIMENTATION COEFFICIENTS; SEDIMENTATION EQUILIBRIUM ANALYSIS; SEDIMENTATION VELOCITIES; SELF-ASSOCIATIONS; SOLUTION CONDITIONS;

AMINO ACIDS; DIMERIZATION; DIMERS; HYDRODYNAMICS; MONOMERS; SEDIMENTS;

ASSOCIATION REACTIONS;

ISOPROTEIN; PROGESTERONE RECEPTOR;

ARTICLE; CHEMISTRY; DIMERIZATION; GENETICS; HUMAN; METHODOLOGY; PROTEIN TERTIARY STRUCTURE; ULTRACENTRIFUGATION;

DIMERIZATION; HUMANS; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, PROGESTERONE; ULTRACENTRIFUGATION;

EID: 33750715148     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi0612317     Document Type: Article

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