13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.

doi:10.1016/S0006-3495(94)81006-9

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Article

13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.

Biophysical journal - 1 Jun 1994

Kemple M D, Yuan P, Nollet K E, Fuchs J A, Silva N, Prendergast F G

Abstract excerpt

The rotational motion of tryptophan side chains in oxidized and reduced wild-type (WT) Escherichia coli thioredoxin and in two single-tryptophan variants of E. coli thioredoxin was studied in solution in the temperature range 20-50 degrees C from 13C-NMR relaxation rate measurements at 75.4 and 1...

Topics

Carbon Isotopes
Escherichia coli
Fluorescence Polarization
Genetic Variation
Magnetic Resonance Spectroscopy
Mathematics
Models, Molecular
Models, Theoretical
Mutagenesis, Site-Directed
Oxidation-Reduction
Point Mutation
Protein Conformation
Recombinant Proteins
Restriction Mapping

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Identifiers

PMID: 8075345
DOI: 10.1016/S0006-3495(94)81006-9
PMCID: PMC1275937

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8075345-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Thioredoxins

Tryptophan