Key result
In the presence of ATP, actin interacts infrequently and only at restricted sites of the lysine-rich sequence of myosin, whereas it interacts fully over the whole length in the rigor state.
The N-terminal acidic sequence of actin interacts infrequently and at restricted sites of the lysine-rich sequence of myosin in the weakly binding state (with ATP), but interacts fully over the whole length in the rigor state (without ATP).
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Informs weak-binding models of cardiac myosin; leaves open relevance to human sarcomere function and disease.
Keiichi Yamamoto (1989) studied this question. ATP vs. Absence of ATP was evaluated on Cross-linking of the N-terminal acidic sequence of actin to the lysine-rich sequence of myosin subfragment 1. In the presence of ATP, actin interacts infrequently and only at restricted sites of the lysine-rich sequence of myosin, whereas it interacts fully over the whole length in the rigor state.
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