Quantitative 13C and 2H NMR relaxation studies of the 723-residue enzyme malate synthase G reveal a dynamic binding interface

Biochemistry

Volumn 44, Issue 49, 2005, Pages 15970-15977

  Tugarinov, Vitali ^a   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; NUCLEAR MAGNETIC RESONANCE; PROTEINS; SUBSTRATES;

ANTIBIOTIC AGENTS; MOLECULAR RECOGNITION; MSG;

ENZYMES;

ANTIBIOTIC AGENT; ISOLEUCINE; LEUCINE; MALATE SYNTHASE; MALATE SYNTHASE G; METHYL GROUP; UNCLASSIFIED DRUG; VALINE; ACETYL COENZYME A; CARBON; DEUTERIUM; ISOENZYME; PYRUVIC ACID;

ARTICLE; BINDING AFFINITY; BINDING SITE; CARBON NUCLEAR MAGNETIC RESONANCE; CONFORMATIONAL TRANSITION; CORRELATION COEFFICIENT; DEUTERON NUCLEAR MAGNETIC RESONANCE; DRUG TARGETING; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; LIGAND BINDING; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR WEIGHT; PARAMETER; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; STRUCTURE ANALYSIS; TECHNIQUE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION;

ACETYL COENZYME A; BINDING SITES; CARBON ISOTOPES; DEUTERIUM; ISOENZYMES; ISOLEUCINE; LEUCINE; MALATE SYNTHASE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PYRUVIC ACID; VALINE;

EID: 28944442463     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0519809     Document Type: Article

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