Distance mapping in proteins using fluorescence spectroscopy

Tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner

Amber M. Jones Brunette, David Farrens

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Tryptophan-induced quenching of fluorophores (TrIQ) uses intramolecular fluorescence quenching to assess distances in proteins too small (a) to this movement is relatively low (∼1.5-2.5 kcal/mol). Together, these results demonstrate that TyrIQ, used together with TrIQ, significantly expands the power of quenching-based distance mapping SDFL studies.

Original languageEnglish (US)
Pages (from-to)6290-6301
Number of pages12
JournalBiochemistry
Volume53
Issue number40
DOIs
StatePublished - Oct 14 2014

Fingerprint

Fluorescence Spectrometry
Fluorescence spectroscopy
Tryptophan
Tyrosine
Quenching
Fluorescence
Fluorophores
Proteins
bimanes

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

Cite this

Distance mapping in proteins using fluorescence spectroscopy : Tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner. / Jones Brunette, Amber M.; Farrens, David.

In: Biochemistry, Vol. 53, No. 40, 14.10.2014, p. 6290-6301.

Research output: Contribution to journalArticle

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