Key result
Adding ±5-degree actin torsional fluctuations improves lever arm model predictions of myosin V step sizes.
Why the study?
The influence of helical disorder in the actin structure on myosin V step size and its agreement with experimental data was unclear.
No immediate clinical relevance; leaves open broader validation of torsional adjustments across motor proteins.
We study the influence of helical disorder in the actin structure on the myosin V step size, predicted from the elastic lever arm model. We show that fluctuations of +/-5 degrees per actin subunit, as proposed by Egelman et al., significantly alter the distribution of step sizes and improve the agreement with experimental data.
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Andrej Vilfan (2005) studied Myosin V motility. Torsional fluctuations in actin structure (±5 degrees per subunit) vs. Stiff 13/6 actin helix was evaluated on Myosin V step size distribution. Incorporating torsional fluctuations of ±5 degrees per actin subunit into the elastic lever arm model significantly alters the predicted distribution of myosin V step sizes, improving agreement with experimental data.
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