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Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-
19
F-tryptophan-labeled Escherichia coli dihydrofolate reductase
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 (ICTS)
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
107
Scopus citations
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Dive into the research topics of 'Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-
19
F-tryptophan-labeled Escherichia coli dihydrofolate reductase'. Together they form a unique fingerprint.
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Keyphrases
Stopped Flow
100%
Tryptophan
100%
NMR Spectroscopy
100%
Escherichia Coli Dihydrofolate Reductase
100%
Flow NMR
100%
Circular Dichroism
50%
NMR Data
50%
Urea-induced Unfolding
50%
Native-like
25%
Side Chain
25%
19F NMR
25%
Circular Dichroism Spectroscopy
25%
Slow Phase
25%
Secondary Structure
25%
Tryptophan Residues
25%
19F NMR Spectroscopy
25%
Native Protein
25%
Unfolded State
25%
Stopped-flow Technique
25%
NMR Assignment
25%
Far-UV Circular Dichroism
25%
Structural Form
25%
Total Intensity
25%
Biochemistry, Genetics and Molecular Biology
Escherichia coli
100%
Dihydrofolate Reductase
100%
Tryptophan
100%
Nuclear Magnetic Resonance Spectroscopy
100%
Circular Dichroism
60%
Protein Secondary Structure
20%