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27 August 2010 Breaking of bonds between a kinesin motor and microtubules causes protein friction
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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.
© (2010) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Volker Bormuth, Vladimir Varga, Jonathon Howard, and Erik Schäffer "Breaking of bonds between a kinesin motor and microtubules causes protein friction", Proc. SPIE 7762, Optical Trapping and Optical Micromanipulation VII, 776208 (27 August 2010);

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