Abstract
The room temperature tryptophan phosphorescence (RTTP) technique allows studying slow internal dynamics of proteins in the millisecond and second diapasons. This chapter summarizes the key findings in the field of RTTP spectroscopy, physical nature of this phenomenon, and experimental approaches to analyze the microenvironment of tryptophan residues. Representative examples of RTTP of proteins in human erythrocyte membranes and plant lectins in solutions are discussed in details taking into account the effects of detergents on biological membranes and 3D structures of lectin molecules, respectively.
Keywords
- Critical Micelle Concentration
- Protein Data Bank
- Erythrocyte Membrane
- Tryptophan Residue
- Wheat Germ Agglutinin
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Mazhul’, V.M., Timoshenko, A.V., Zaitseva, E.M., Loznikova, S.G., Halets, I.V., Chernovets, T.S. (2010). Room Temperature Tryptophan Phosphorescence of Proteins in the Composition of Biological Membranes and Solutions. In: Geddes, C.D. (eds) Reviews in Fluorescence 2008. Reviews in Fluorescence 2008, vol 2008. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-1260-2_2
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