ArticleBiophysical journal2001
Theoretical kinetic studies of models for binding myosin subfragment-1 to regulated actin: Hill model versus Geeves model.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Negative Charges Introduced Near the IT Helix of Cardiac Troponin T Stabilize the Active State of Actin Filaments.Biochemistry · 2023Article
- Review
- The mechanism of thin filament regulation: Models in conflict?The Journal of general physiology · 2019Review
- Stepwise C-Terminal Truncation of Cardiac Troponin T Alters Function at Low and Saturating CaBiophysical journal · 2018Article
- Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Biochemistry · 2017Article
- Disease causing mutations of troponin alter regulated actin state distributions.Journal of muscle research and cell motility · 2012Review
- Cooperative regulation of myosin-S1 binding to actin filaments by a continuous flexible Tm-Tn chain.European biophysics journal : EBJ · 2012Article
- The Hill model for binding myosin S1 to regulated actin is not equivalent to the McKillop-Geeves model.Journal of molecular biology · 2012Article
- Kinetics of regulated actin transitions measured by probes on tropomyosin.Biophysical journal · 2010Article
- Resolution and uniqueness of estimated parameters of a model of thin filament regulation in solution.Computational biology and chemistry · 2010Article
- The regulation of myosin binding to actin filaments by Lethocerus troponin.Journal of molecular biology · 2007Article
- Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments.Journal of muscle research and cell motility · 2007Article
- The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin.Biochemistry · 2004Article
- Ca2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications.Biophysical journal · 2004Article
- Cooperative regulation of myosin-actin interactions by a continuous flexible chain I: actin-tropomyosin systems.Biophysical journal · 2003Article
- Troponin-tropomyosin: an allosteric switch or a steric blocker?Biophysical journal · 2002Article
- Cooperative behavior of molecular motors.Journal of muscle research and cell motility · 2002Review
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4 authors.
Funding
Abstract
It was previously shown that a one-dimensional Ising model could successfully simulate the equilibrium binding of myosin S1 to regulated actin filaments (T. L. Hill, E. Eisenberg and L. Greene, Proc. Natl. Acad. Sci. U.S.A. 77:3186-3190, 1980). However, the time course of myosin S1 binding to regulated actin was thought to be incompatible with this model, and a three-state model was subsequently developed (D. F. McKillop and M. A. Geeves, Biophys. J. 65:693-701, 1993). A quantitative analysis of the predicted time course of myosin S1 binding to regulated actin, however, was never done for either model. Here we present the procedure for the theoretical evaluation of the time course of myosin S1 binding for both models and then show that 1) the Hill model can predict the "lag" in the binding of myosin S1 to regulated actin that is observed in the absence of Ca++ when S1 is in excess of actin, and 2) both models generate very similar families of binding curves when [S1]/[actin] is varied. This result shows that, just based on the equilibrium and pre-steady-state kinetic binding data alone, it is not possible to differentiate between the two models. Thus, the model of Hill et al. cannot be ruled out on the basis of existing pre-steady-state and equilibrium binding data. Physical mechanisms underlying the generation of the lag in the Hill model are discussed.
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