Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures

F Tölgyesi; B Ullrich; J Fidy

doi:10.1016/s0167-4838(99)00200-9

Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures

Biochim Biophys Acta. 1999 Nov 16;1435(1-2):1-6. doi: 10.1016/s0167-4838(99)00200-9.

Authors

F Tölgyesi¹, B Ullrich, J Fidy

Affiliation

¹ Institute of Biophysics, Semmelweis University of Medicine, Puskin u. 9., Budapest, Hungary. [email protected]

PMID: 10561532
DOI: 10.1016/s0167-4838(99)00200-9

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alkaline Phosphatase / chemistry
Apoproteins / chemistry
Azurin / chemistry
Body Temperature
Crystallins / chemistry
Luminescent Measurements
Proteins / chemistry*
Temperature*
Thermodynamics
Tryptophan / chemistry*

Substances

Apoproteins
Crystallins
Proteins
apoazurin
Azurin
Tryptophan
Alkaline Phosphatase