Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures

Ferenc Tölgyesi, Beáta Ullrich, Judit Fidy

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The Arrhenius plot of the de-excitation rate of tryptophan triplet state deviates from linearity in the physiological temperature range for several proteins with buried tryptophans, similarly to the behaviour of enzyme activity. A model is presented featuring two de-excitation pathways whose effectiveness is regulated by protein dynamics.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1435
Issue number1-2
DOIs
Publication statusPublished - Nov 16 1999

Keywords

  • Alkaline phosphatase
  • Apoazurin
  • Liver alcohol dehydrogenase
  • Non-Arrhenius temperature dependence
  • Water quenching
  • α-Crystallin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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