Tryptophan phosphorescence signals characteristic changes in protein dynamics at physiological temperatures
| Autor: | Judit Fidy, Beáta Ullrich, Ferenc Tölgyesi |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Biophysics
macromolecular substances Photochemistry Biochemistry Body Temperature Azurin Structural Biology Triplet state Molecular Biology biology Chemistry Protein dynamics Temperature Tryptophan Proteins Atmospheric temperature range Alkaline Phosphatase Crystallins Enzyme assay Arrhenius plot Luminescent Measurements biology.protein Thermodynamics Apoproteins Phosphorescence |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1435:1-6 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/s0167-4838(99)00200-9 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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