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19
F NMR Spectroscopy of [6-
19
F]Tryptophan-Labeled Escherichia coli Dihydrofolate Reductase: Equilibrium Folding and Ligand Binding Studies
Sydney D. Hoeltzli,
Carl Frieden
Department of Biochemistry & Molecular Biophysics
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
Institute of Clinical and Translational Sciences
Bursky Center for Human Immunology & Immunotherapy Programs (CHiiPs)
Research output
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Contribution to journal
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Article
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peer-review
45
Scopus citations
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19
F NMR Spectroscopy of [6-
19
F]Tryptophan-Labeled Escherichia coli Dihydrofolate Reductase: Equilibrium Folding and Ligand Binding Studies'. Together they form a unique fingerprint.
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Chemical Compounds
Dihydrofolates
94%
19F NMR Spectroscopy
84%
Tryptophan
69%
Resonance
52%
Apoprotein
50%
Methotrexate
41%
19F NMR Spectrum
33%
Urea
26%
Chemical Shift
19%
Tryptophan Residue
18%
Protein
13%
Phenylalanine
8%
Denaturation
7%
Binding Site
5%
Crystal Structure
4%
Ligand
3%
Medicine & Life Sciences
Tetrahydrofolate Dehydrogenase
100%
Tryptophan
79%
Magnetic Resonance Spectroscopy
62%
Ligands
52%
Escherichia coli
52%
Apoproteins
45%
NADP
44%
Methotrexate
26%
Urea
25%
6-fluorotryptophan
14%
Proteins
10%
Phenylalanine
7%
Binding Sites
5%
Enzymes
3%