Conformational kinetics reveals affinities of protein conformational states

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

Volumn 112, Issue 30, 2015, Pages 9352-9357

  Daniels, Kyle G ^a   Suo, Yang ^a   Oas, Terrence G ^a  

^a DUKE UNIVERSITY   (United States)

Author keywords

Allostery; Binding; Change; Conformational; Coupled

Indexed keywords

GLYCINE DEHYDROGENASE (DECARBOXYLATING); BACTERIAL PROTEIN; LIGAND; MACROMOLECULE; PROTEIN BINDING; RIBONUCLEASE P;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; FLUORESCENCE; ISOTHERMAL TITRATION CALORIMETRY; KINETICS; LIGAND BINDING; LIMIT OF DETECTION; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; CALORIMETRY; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DESIGN; MACROMOLECULE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; THERMODYNAMICS;

ALLOSTERIC SITE; BACTERIAL PROTEINS; BINDING SITES; CALORIMETRY; DRUG DESIGN; KINETICS; LIGANDS; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; RIBONUCLEASE P; THERMODYNAMICS;

EID: 84938099079     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1502084112     Document Type: Article

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