Abstract
High-speed atomic force microscopy (HS-AFM) is a unique tool that enables imaging of protein molecules during their functional activity at sub-100 ms temporal and submolecular spatial resolution. HS-AFM is suited for the study of highly dynamic proteins, including myosin motors. HS-AFM images of myosin V walking on actin filaments provide irrefutable evidence for the swinging lever arm motion propelling the molecule forward. Moreover, molecular behaviors that have not been noticed before are also displayed on the AFM movies. This chapter describes the principle, underlying techniques and performance of HS-AFM, filmed images of myosin V, and mechanistic insights into myosin motility provided from the filmed images.
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Acknowledgements
We thank Takayuki Uchihashi, Daisuke Yamamoto, Ryoki Ishikawa, Takeshi Sakamoto, Tatsuya Kinoshita and Hiroshi Koide for useful discussions and technical assistances. This work was supported by JSPS KAKENHI (JP22870011 and 24770149 to N.K; JP24227005, JP26119003 and 17H06121 to T.A.) and JST grant (JPMJPR13L4 and JPMJCR1762 to N.K.; JPMJCR13M1 to T.A.).
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Kodera, N., Ando, T. (2020). High-Speed Atomic Force Microscopy to Study Myosin Motility. In: Coluccio, L. (eds) Myosins. Advances in Experimental Medicine and Biology, vol 1239. Springer, Cham. https://doi.org/10.1007/978-3-030-38062-5_7
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DOI: https://doi.org/10.1007/978-3-030-38062-5_7
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