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Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures
F Tölgyesi1, B Ullrich, J Fidy
1Institute of Biophysics, Semmelweis University of Medicine, Puskin u. 9., Budapest, Hungary. tolgyesi@puskin.sote.hu
Biochimica Et Biophysica Acta
|November 24, 1999
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.