Phosphorescence of tryptophan from parvalbumin and actin in liquid solution
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(82)81013-2/fullpdf
Reference8 articles.
1. Room Temperature Phosphorescence and the Dynamic Aspects of Protein Structure
2. HETEROGENEITY IN THE THERMALLY-INDUCED QUENCHING OF THE PHOSPHORESCENCE OF MULTI-TRYPTOPHAN PROTEINS
3. TEMPERATURE DEPENDENCE OF THE PHOSPHORESCENCE LIFETIMES OF HETEROGENEOUS TRYPTOPHAN RESIDUES IN GLOBULAR PROTEINS BETWEEN 293 AND 77 K
4. Lanthanide ion luminescence probes. Measurement of distance between intrinsic protein fluorophores and bound metal ions: quantitation of energy transfer between tryptophan and terbium(III) or europium(III) in the calcium-binding protein parvalbumin
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3. Intramolecular Quenching of Tryptophan Phosphorescence in Short Peptides and Proteins¶;Photochemistry and Photobiology;2007-04-30
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