Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories 1 1Edited by P. E. Wright
- 1 January 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 315 (2) , 239-251
- https://doi.org/10.1006/jmbi.2001.5218
Abstract
No abstract availableKeywords
This publication has 62 references indexed in Scilit:
- The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobinProceedings of the National Academy of Sciences, 2001
- The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobinBiophysical Journal, 1994
- The Energy Landscapes and Motions of ProteinsScience, 1991
- Rate Theories and Puzzles of Hemeprotein KineticsScience, 1985
- THE DEPENDENCE OF THE QUANTUM YIELD OF LIGAND PHOTODISSOCIATION FROM HAEM PROTEINS ON ULTRAFAST RECOMBINATIONPhotochemistry and Photobiology, 1980
- Transient Raman study of CO–haemoprotein photolysis: origin of the quantum yieldNature, 1980
- Transient effects in the nanosecond laser photolysis of carboxyhemoglobin: “CAGE” recombination annd spectral evolution of the proteinChemical Physics Letters, 1979
- Dynamics of ligand binding to myoglobinBiochemistry, 1975
- Dynamics of Carbon Monoxide Binding by Heme ProteinsScience, 1973
- Carbon Monoxide Binding by Hemoglobin and Myoglobin under Photodissociating ConditionsProceedings of the National Academy of Sciences, 1972