Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures

Citation
F. Tolgyesi et al., Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures, BBA-PROT ST, 1435(1-2), 1999, pp. 1-6
Citations number
33
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
ISSN journal
01674838 → ACNP
Volume
1435
Issue
1-2
Year of publication
1999
Pages
1 - 6
Database
ISI
SICI code
0167-4838(19991116)1435:1-2<1:TPSCCI>2.0.ZU;2-P
Abstract
The Arrhenius plot of the de-excitation rate of tryptophan triplet state de viates from linearity in the physiological temperature range for several pr oteins with buried tryptophans, similarly to the behaviour of enzyme activi ty. A model is presented featuring two de-excitation pathways whose effecti veness is regulated by protein dynamics. (C) 1999 Elsevier Science B.V. All rights reserved.