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Use of Photonic Force Microscopy to Study Single-Motor-Molecule Mechanics

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Kinesin Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 164))

Abstract

With the intensive study of functional properties of motor proteins at the single-molecule level, many new insights were gained on the correlation between the kinesin structure and its function. Recent work on kinesins has demonstrated that the neck and the first hinge region of the motor play an important role in kinesin directionality, velocity, and ATPase activity (14). The investigation of the three-dimensional (3D) mechanical properties in this context can provide the information to understand how structural changes stipulate the molecular function. A 3D view is essential, as mechanical properties can be anisotropic and motor molecules, in general, move in space to fulfill their function.

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© 2001 Humana Press Inc.

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Jeney, S., Florin, EL., Heinrich Hörber, J.K. (2001). Use of Photonic Force Microscopy to Study Single-Motor-Molecule Mechanics. In: Vernos, I. (eds) Kinesin Protocols. Methods in Molecular Biology™, vol 164. Humana Press. https://doi.org/10.1385/1-59259-069-1:91

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  • DOI: https://doi.org/10.1385/1-59259-069-1:91

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-766-3

  • Online ISBN: 978-1-59259-069-8

  • eBook Packages: Springer Protocols

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