Cryoenzymic studies on myosin: transient kinetic evidence for two types of head with different ATP binding properties
- 1 March 1989
- Vol. 71 (3), 363-372
- https://doi.org/10.1016/0300-9084(89)90008-4
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Transient kinetics of the interaction of 1,N6-ethenoadenosine 5'-triphosphate with myosin subfragment 1 under normal and cryoenzymic conditions: a comparison with adenosine 5'-triphosphateBiochemistry, 1988
- RELATIONSHIPS BETWEEN CHEMICAL AND MECHANICAL EVENTS DURING MUSCULAR CONTRACTIONAnnual Review of Biophysics, 1986
- The Rapid‐Flow‐Quench Method in the Study of Fast Reactions in Biochemistry: Extension to Subzero ConditionsPublished by Wiley ,1985
- Transient kinetics of ADP and AMP-PNP binding to subfragment 1 and actosubfragment 1Biochemistry, 1982
- Regulation and Kinetics of the Actin-Myosin-ATP InteractionAnnual Review of Biochemistry, 1980
- Fluorescence stopped-flow study of the mechanism of nucleotide binding to myosin subfragment 1Biochemistry, 1979
- Structure and Function of the Two Heads of the Myosin MoleculeThe Journal of Biochemistry, 1977
- Edwin Taylor — a single pathway for myosin ATP hydrolysis is sufficient to explain all the dataTrends in Biochemical Sciences, 1977
- Kinetic Analysis of ATPase MechanismsQuarterly Reviews of Biophysics, 1976
- The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociationBiochemical Journal, 1974