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Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures
Authors:Tölgyesi F  Ullrich B  Fidy J
Affiliation:Institute of Biophysics, Semmelweis University of Medicine, Puskin u. 9., Budapest, Hungary. tolgyesi@puskin.sote.hu
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.
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