The application of nanosecond fluorometry to an allosteric protein
- 8 April 1974
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 57 (3), 876-886
- https://doi.org/10.1016/0006-291x(74)90628-7
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Influence of substrate and effectors on the binding of 1-anilino-8-naphthalenesulfonate by glycogen phosphorylaseBiochemistry, 1972
- Probes for the Conformational Transitions of Phosphorylase bEuropean Journal of Biochemistry, 1971
- The Analysis of Fluorescence Decay by a Method of MomentsBiophysical Journal, 1969
- Effect of temperature on the allosteric transitions of rabbit skeletal muscle phosphorylase bBiochemistry, 1968
- Fluorescence Spectroscopy of ProteinsScience, 1968
- Subunit interactions and their relation to the allosteric properties of rabbit skeletal muscle phosphorylase bBiochemistry, 1968
- Fluorescent Probes for Conformational States of Proteins. III. The Activation of Chymotrypsinogen*Biochemistry, 1967
- Fluorescent Probes for Conformational States of Proteins. II. The Binding of 2-p-Toluidinylnaphthalene-6-sulfonate to α-Chymotrypsin*Biochemistry, 1967
- Fluorescent Probes for Conformational States of Proteins. I. Mechanism of Fluorescence of 2-p-Toluidinylnaphthalene-6-sulfonate, a Hydrophobic Probe*Biochemistry, 1966
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965