Electrostatic contributions to the binding of myosin and myosin-MgADP to F-actin in solution.
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Summary
The ionic strength dependence of skeletal myosin subfragment 1 (S1) binding to unregulated F-actin was measured in solutions containing from 0 to 0.50 M added lithium acetate in the absence and presence of MgADP to show consistency with a model in which Mg ADP binding to S1 reduces its affinity for actin by a mechanism that reduces the net electric charge of the acting binding site on S1.
- Type
- article
- Published
- 1990-11-27
- Cited by
- 20
- References
- 51
- OpenAlex
- https://openalex.org/W2271676
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:7219192
Keywords
Computer science
References
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- Thermodynamics of electrolytes. IV. Activity and osmotic coefficients for mixed electrolytes
Cited by
- Role of charges in actomyosin interactions.
- Electrostatic potential around actin.
- Human Lymphocyte-Specific Protein 1, the Protein Overexpressed in Neutrophil Actin Dysfunction with 47-kDa and 89-kDa Protein Abnormalities (NAD 47/89), Has Multiple F-Actin Binding Domains1
- Modulation of actomyosin motor function by 1-hexanol
- Poorly Understood Aspects of Striated Muscle Contraction
- Structural relationships of actin-binding proteins.
- Interaction and polymerization of the G-actin-myosin head complex: effect of DNase I.
- Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle.
- In vitro assays of molecular motors--impact of motor-surface interactions.
- Rescue of in vitro actin motility halted at high ionic strength by reduction of ATP to submicromolar levels.
- Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: detection by antibodies against the N-terminal segment of actin.
- Cross-linking myosin subfragment 1 Cys-697 and Cys-707 modifies ATP and actin binding site interactions.
- Temperature-enhanced association of proteins due to electrostatic interaction: a coarse-grained simulation of actin-myosin binding.
- Muscle contraction andin vitro movement: Role of actin?
- Electrostatic forces as a possible mechanism underlying skeletal muscle contraction.
- The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo
- Muscle contraction and in vitro actin? movement: role of
- Materials science and mechanosensitivity of living matter.
- F-Actin Binding Domains Abnormalities (NAD 47/89), Has Multiple Dysfunction with 47-kDa and 89-kDa Protein Protein Overexpressed in Neutrophil Actin Human Lymphocyte-Specific Protein 1, the
- Electrostatic Forces as a Possible Mechanism Underlying Skeletal Muscle Contraction
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