Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 33, 2014, Pages 12055-12060

  Shammas, Sarah L ^a   Travis, Alexandra J ^a   Clarke, Jane ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Coupled folding and binding; Dynamic allostery; Induced fit; Intrinsic disorder; Intrinsically disordered protein

Indexed keywords

CREB BINDING PROTEIN KINASE INDUCIBLE DOMAIN INTERACTING; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; INTRINSICALLY DISORDERED PROTEIN; UNCLASSIFIED DRUG; TRANSACTIVATOR PROTEIN;

ALLOSTERISM; APPARENT ASSOCIATION RATE CONSTANT; ARTICLE; BINDING SITE; COMPARATIVE STUDY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DISSOCIATION RATE CONSTANT; FLUORESCENCE; IONIC STRENGTH; LIGAND BINDING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STATIC ELECTRICITY; SURFACE PROPERTY; TRANSACTIVATION; CHEMICAL STRUCTURE; CHEMISTRY; COUPLED FOLDING AND BINDING; DYNAMIC ALLOSTERY; INDUCED FIT; INTRINSIC DISORDER; KINETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

COUPLED FOLDING AND BINDING; DYNAMIC ALLOSTERY; INDUCED FIT; INTRINSIC DISORDER; INTRINSICALLY DISORDERED PROTEIN;

ALLOSTERIC REGULATION; FLUORESCENCE; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; TRANS-ACTIVATORS;

EID: 84906328511     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1405815111     Document Type: Article

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