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

Keywords

Computer science

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