Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: A stopped-flow NMR spectroscopy study

Biochemistry

Volumn 37, Issue 1, 1998, Pages 387-398

  Hoeltzli, Sydney D ^a   Frieden, Carl ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; DIHYDROFOLIC ACID; FLUORINE; LIGAND; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRYPTOPHAN; DRUG DERIVATIVE; FOLIC ACID;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ENZYMOLOGY; METABOLISM; METHODOLOGY; SPECTROFLUOROMETRY;

CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORINE; FOLIC ACID; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NADP; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TETRAHYDROFOLATE DEHYDROGENASE; TRYPTOPHAN;

EID: 0032488452     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971962u     Document Type: Article

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