Why the study?
Does myosin-substrate interaction in vitro result in a delocalized conformation change?
Does myosin-substrate interaction in vitro result in a delocalized conformation change?
The study demonstrates that myosin-substrate interaction in vitro does not result in a delocalized conformational change.
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Challenges allosteric myosin models; leaves open localized mechanisms of cardiac force generation.
The effect of substrate on the far UV (185-250 nm) and near UV (250-325 nm) circular dichroism (CD) of myosin and heavy meromyosin (HMM) was studied. The following results were obtained with the addition of ATP (during various conditions of hydrolysis), ADP, and pyrophosphate: (1) no changes were observed in the far UV CD, (2) ATP and ADP perturbed the near UV CD only at spectral regions below 280 nm coinciding with the regions of their optical activity, (3) the optically inactive pyrophosphate caused no change in the near UV CD, and (4) myosin and HMM gave exactly the same results. These results suggest that myosin-substrate interaction in vitro does not result in a delocalized conformational change.
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Cassim et al. (1975) studied this question.
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