Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands

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

Volumn 107, Issue 4, 2010, Pages 1373-1378

  Boehr, David D ^a,b   McElheny, Dan ^a,c   Dyson, H Jane ^a   Wright, Peter E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

^c UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

Catalysis; Energy landscape; Enzyme dynamics; NMR; Relaxation

Indexed keywords

DIHYDROFOLATE REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; ENERGY TRANSFER; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; LIGAND BINDING; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; THERMODYNAMICS;

ESCHERICHIA COLI; LIGANDS; MODELS, MOLECULAR; NADP; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TETRAHYDROFOLATE DEHYDROGENASE; TETRAHYDROFOLATES; THERMODYNAMICS; TIME FACTORS;

ESCHERICHIA COLI;

EID: 76549109225     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0914163107     Document Type: Article

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