[4] Time-resolved room temperature tryptophan phosphorescence in proteins
- 1 January 1997
- book chapter
- Published by Elsevier
- Vol. 278, 49-71
- https://doi.org/10.1016/s0076-6879(97)78006-6
Abstract
No abstract availableKeywords
This publication has 70 references indexed in Scilit:
- Phosphorescence Reveals a Continued Slow Annealing of the Protein Core following Reactivation of Escherichia coli Alkaline PhosphataseBiochemistry, 1995
- Pressure Effects on Protein Flexibility Monomeric ProteinsJournal of Molecular Biology, 1994
- Nitric oxide diffusion coefficients in solutions, proteins and membranes determined by phosphorescenceBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- Conformational changes in proteins induced by dynamic associations. A tryptophan phosphorescence studyEuropean Journal of Biochemistry, 1994
- The Role of Solvent Viscosity in the Dynamics of Protein Conformational ChangesScience, 1992
- Intrinsic tryptophan phosphorescence as a marker of conformation and oxygen diffusion in purified cytochrome oxidaseFEBS Letters, 1991
- TRYPTOPHAN PHOSPHORESCENCE AT ROOM TEMPERATURE AS A TOOL TO STUDY PROTEIN STRUCTURE AND DYNAMICSPhotochemistry and Photobiology, 1989
- Quenching of room temperature protein phosphorescence by added small moleculesBiochemistry, 1988
- Determination of the dioxygen quenching constant for protein and model indole tripletsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Conformation heterogeneity in proteins as an origin of heterogeneous fluorescence decays, illustrated by native and denatured ribonuclease T1Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988