title: Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures.
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.
authors.affiliation: Institute of Biophysics, Semmelweis University of Medicine, Puskin u. 9., Budapest, Hungary. tolgyesi@puskin.sote.hu
authors.forename: F
authors.initials: F
authors.lastname: Tölgyesi
authors.forename: B
authors.initials: B
authors.lastname: Ullrich
authors.forename: J
authors.initials: J
authors.lastname: Fidy
mesh_terms: 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*
chemical_list: D001059:Apoproteins; D003459:Crystallins; D011506:Proteins; C038778:apoazurin; D001400:Azurin; D014364:Tryptophan; D000469:Alkaline Phosphatase