Abstract
Actomyosin is a protein complex composed of myosin and actin, which is well known for being the minimal contractile unit of muscle. The chemical free energy of ATP is converted into mechanical work by the complex, and the single-molecule mechanical properties of myosin are well characterized in vitro. However, the aqueous solution environment in in vitro assay is far from that in cells, where biomolecules are crowded, which influences osmotic pressure, and processes such as folding, and association and diffusion of proteins. Here, to bridge the gap between in vitro and in-cell environment, we observed mechanical motion of actomyosin-V in the presence of the osmolyte sucrose, as a model system. Single-molecule observation of myosin-V motor domains (heads) on actin filament at varying sucrose concentration revealed modulated mechanical elementary processes suggesting increased affinity of heads with actin and more robust force generation possibly accompanied by a sliding motion of myosin head along actin.
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Iwaki, M., Ito, K., Fujita, K. (2018). Single-Molecule Analysis of Actomyosin in the Presence of Osmolyte. In: Suzuki, M. (eds) The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer, Singapore. https://doi.org/10.1007/978-981-10-8459-1_15
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DOI: https://doi.org/10.1007/978-981-10-8459-1_15
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