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Proceedings Paper

Breaking of bonds between a kinesin motor and microtubules causes protein friction
Author(s): Volker Bormuth; Vladimir Varga; Jonathon Howard; Erik Schäffer
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Paper Abstract

Friction limits the operation of macroscopic machines. Using optical tweezers, we showed that friction also limits the operation of molecular machines by measuring the friction between single yeast kinesin-8, Kip3p, and its microtubule track. The protein friction arises from the force necessary to break the adhesive bonds that Kip3p forms with discretely, 8-nm spaced binding sites on its track. A model based on bond rupture dynamics with a single energy barrier described the data. A uctuation analysis confirmed Kip3p stepping during diffusion. Here, we validate our experimental results and data analysis by a Monte Carlo simulation. Our data have implications for other molecular machines or actively driven proteins, and give further insight into diffusion of proteins along polymers such as microtubules or DNA.

Paper Details

Date Published: 27 August 2010
PDF: 7 pages
Proc. SPIE 7762, Optical Trapping and Optical Micromanipulation VII, 776208 (27 August 2010); doi: 10.1117/12.863545
Show Author Affiliations
Volker Bormuth, Max-Planck-Institut für molekulare Zellbiologie und Genetik (Germany)
Vladimir Varga, Max-Planck-Institut für molekulare Zellbiologie und Genetik (Germany)
Jonathon Howard, Max-Planck-Institut für molekulare Zellbiologie und Genetik (Germany)
Erik Schäffer, Technische Univ. Dresden (Germany)


Published in SPIE Proceedings Vol. 7762:
Optical Trapping and Optical Micromanipulation VII
Kishan Dholakia; Gabriel C. Spalding, Editor(s)

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