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Proceedings Article

Breaking of bonds between a kinesin motor and microtubules causes protein friction

[+] Author Affiliations
Volker Bormuth, Vladimir Varga, Jonathon Howard

Max-Planck-Institut für molekulare Zellbiologie und Genetik (Germany)

Erik Schäffer

Technische Univ. Dresden (Germany)

Proc. SPIE 7762, Optical Trapping and Optical Micromanipulation VII, 776208 (August 27, 2010); doi:10.1117/12.863545
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From Conference Volume 7762

  • Optical Trapping and Optical Micromanipulation VII
  • Kishan Dholakia; Gabriel C. Spalding
  • San Diego, California | August 01, 2010

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.

© (2010) COPYRIGHT SPIE--The International Society for Optical Engineering. Downloading of the abstract is permitted for personal use only.
Citation

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 (August 27, 2010); doi:10.1117/12.863545; http://dx.doi.org/10.1117/12.863545


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