Key result
Optical tweezers revealed that in both nucleotide-free and ADP-bound states, single- and double-headed binding of myosin V to actin occurs with approximately the same probability.
Optical nanometry using optical tweezers can reliably study the interaction mechanisms of cytoskeleton molecular motors like myosin V with actin filaments.
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The interaction between actin and myosin V has been probed by measuring the unbinding force of individual actomyosin complexes using optical tweezers. Surprisingly, we found that in both the nucleotide-free and ADP-bound states single- and double-headed binding occurs with approximately the same probability. Estimation of the spring constant of individual actomyosin complexes confirmed that in each of the nucleotide states two distinct populations exist. These results confirm that optical nanometry can be used to reliably study the mechanism of how cytoskeleton molecular motors interact with their associated polymer lattices under solution conditions more closely resembling the intracellular environment.
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Should not yet guide cardiac myosin-targeted therapies; leaves open predominant binding mode in physiological settings.
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Mikhailenko et al. (2008) studied this question. Optical tweezers was evaluated on Unbinding force of individual actomyosin complexes. Optical tweezers revealed that in both nucleotide-free and ADP-bound states, single- and double-headed binding of myosin V to actin occurs with approximately the same probability.
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