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19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies

Biochemistry

May 10, 1994

S D Hoeltzli, C Frieden

Abstract

Escherichia coli dihydrofolate reductase contains five tryptophan residues distributed throughout its structure. In order to examine the regions of the protein surrounding these tryptophan residues, we have incorporated 6-fluorotryptophan into the protein. To assign the five resonances ...read more

Mentioned in this Paper

Tryptophan
In Vivo NMR Spectroscopy
Alkalescens-Dispar Group
Ligand Binding
Carmol
Complex (molecular entity)
Mutagenesis, Site-Directed
Ligand Binding Domain
Oligonucleotide Primers
Protein Conformation
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19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies

Biochemistry

May 10, 1994

S D Hoeltzli, C Frieden

PMID: 8180172

DOI: 10.1021/bi00184a019

Abstract

Escherichia coli dihydrofolate reductase contains five tryptophan residues distributed throughout its structure. In order to examine the regions of the protein surrounding these tryptophan residues, we have incorporated 6-fluorotryptophan into the protein. To assign the five resonances ...read more

Mentioned in this Paper

Tryptophan
In Vivo NMR Spectroscopy
Alkalescens-Dispar Group
Ligand Binding
Carmol
Complex (molecular entity)
Mutagenesis, Site-Directed
Ligand Binding Domain
Oligonucleotide Primers
Protein Conformation

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