Binding of SH1−SH2-Modified Myosin Subfragment-1 to Actin

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Structured PICO

Population

Myosin subfragment-1 (S1) and F-actin (in vitro biochemical model)

Intervention

Modification of S1 with NPM (in the presence of ATP) or pPDM (in the presence of ADP) at 0 degrees C

Comparator

Unmodified (control) S1

Outcome

Binding constants to actin in the presence and absence of MgATPsurrogate

Covalent linkage of SH1 and SH2 in myosin S1 may be necessary to inhibit the weakly to strongly binding conformational change to actin.

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SH1-SH2 linkage may sustain weak myosin-actin binding without ATP; hypothesis-generating for cardiac contractility mechanisms.

Xie et al. (1998) studied this question.

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