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Article

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.

The journal of physical chemistry. B - 7 Sept 2006

Kim Judy E, Arjara Gitrada, Richards John H, Gray Harry B, Winkler Jay R

Abstract excerpt

Steady-state and time-resolved fluorescence measurements on each of five native tryptophan residues in full-length and truncated variants of E. coli outer-membrane protein A (OmpA) have been made in folded and denatured states. Tryptophan singlet excited-state lifetimes are multiexponential and vary among the residues. In addition, substantial increases in excited-state lifetimes accompany OmpA folding, with...

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Identifiers

PMID: 16942111
DOI: 10.1021/jp061991r
PMCID: PMC2519049

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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