n-Mer binding on a one-dimensional lattice of two-statem-site cells: Heavy meromyosin on regulated actin as an example
- 1 July 1981
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 20 (7) , 1399-1411
- https://doi.org/10.1002/bip.1981.360200704
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
- 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
- Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi.Journal of Biological Chemistry, 1980
- The binding of heavy meromyosin to F-actin.Journal of Biological Chemistry, 1980
- Binding of monovalent and divalent myosin fragments onto sites on actinNature, 1978
- Cooperative interactions in single‐strand oligomers of adenylic acidBiopolymers, 1966
- Some generalized order-disorder transformationsMathematical Proceedings of the Cambridge Philosophical Society, 1952