An extrinsic room temperature phosphorescent probe. Remarkable shielding of benzophenone triplet at the active site of chymotrypsin
- 1 September 1980
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 96 (1) , 106-113
- https://doi.org/10.1016/0006-291x(80)91187-0
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- Phosphorescence evidence for the role of solvent–protein interactions in the energetics of conformational flexibility of liver alcohol dehydrogenaseCanadian Journal of Biochemistry, 1979
- Fluorescence Energy Transfer as a Spectroscopic RulerAnnual Review of Biochemistry, 1978
- [10] Solute quenching of protein fluorescencePublished by Elsevier ,1978
- Organic Fluorescence Reagents in the Study of Enzymes and ProteinsAngewandte Chemie International Edition in English, 1977
- A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 2: Determination of rotational correlation times of proteins in solutionBiochemistry, 1976
- A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 1: Preparation and properties of a triplet probeBiochemistry, 1976
- Kinetics of triplet–triplet energy transfer and intramolecular distances in enzyme–inhibitor complexesNature, 1976
- The construction of an electronically compensated spectrofluorophosphorimeterJournal of Physics E: Scientific Instruments, 1975
- [24] Nanosecond fluorescence spectroscopy of macromoleculesPublished by Elsevier ,1972
- On the triplet states of polynucleotide–acridine complexes. I. Triplet energy delocalization in the 9‐aminoacridine–DNA complexBiopolymers, 1968