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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 125.7 MHz and at 20 degrees C from steady-state and time-resolved trp fluorescence anisotropy measurements. Tryptophan...

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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 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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