Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures.
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.
Tölgyesi
F
F
Institute of Biophysics, Semmelweis University of Medicine, Puskin u. 9., Budapest, Hungary. tolgyesi@puskin.sote.hu
Ullrich
B
B
Fidy
J
J
D000469:Alkaline Phosphatase / Q000737:chemistry; D001059:Apoproteins / Q000737:chemistry; D001400:Azurin / Q000737:chemistry; D001831:Body Temperature; D003459:Crystallins / Q000737:chemistry; D008163:Luminescent Measurements; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry*
D001059:Apoproteins; D003459:Crystallins; D011506:Proteins; C038778:apoazurin; D001400:Azurin; D014364:Tryptophan; D000469:Alkaline Phosphatase