Two-step ligand binding and cooperativity. A model to describe the cooperative binding of myosin subfragment 1 to regulated actin
- 1 August 1987
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 52 (2) , 215-220
- https://doi.org/10.1016/s0006-3495(87)83208-3
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment 1 from rabbit skeletal muscle. Evidence for two states of acto-subfragment 1Biochemical Journal, 1985
- The effect of nucleotide on the binding of myosin subfragment 1 to regulated actin.Journal of Biological Chemistry, 1982
- Evidence for cross-bridge attachment in relaxed muscle at low ionic strength.Proceedings of the National Academy of Sciences, 1982
- Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.Journal of Biological Chemistry, 1982
- Kinetic studies of the cooperative binding of subfragment 1 to regulated actin.Proceedings of the National Academy of Sciences, 1980
- Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex.Proceedings of the National Academy of Sciences, 1980
- Regulation and Kinetics of the Actin-Myosin-ATP InteractionAnnual Review of Biochemistry, 1980
- Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.Proceedings of the National Academy of Sciences, 1980
- Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting musclesJournal of Molecular Biology, 1973
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965