proceeding · 01/01/2010
Breaking of bonds between a kinesin motor and microtubules causes protein friction
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 fluctuation analysis con firmed 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.
Cite this article
Bormuth, V., Varga, V., Howard, J., & Schaeffer, E. (2010). Breaking of bonds between a kinesin motor and microtubules causes protein friction. OPTICAL TRAPPING AND OPTICAL MICROMANIPULATION VII, 7762(776208). https://doi.org/10.1117/12.863545@inproceedings{Bormuth2010_135,
author = {Bormuth, Volker and Varga, Vladimir and Howard, Jonathon and Schaeffer, Erik},
year = {2010},
month = {1},
title = {Breaking of bonds between a kinesin motor and microtubules causes protein friction},
booktitle = {OPTICAL TRAPPING AND OPTICAL MICROMANIPULATION VII},
publisher = {SPIE-INT SOC OPTICAL ENGINEERING},
volume = {7762},
number = {776208},
series = {Proceedings of SPIE-The International Society for Optical Engineering},
address = {1000 20TH ST, PO BOX 10, BELLINGHAM, WA 98227-0010 USA},
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 fluctuation analysis con firmed 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.},
note = {Conference on Optical Trapped and Optical Micromanipulation VII, San Diego, CA, AUG 01-05, 2010},
url = {http://www.dx.doi.org/10.1117/12.863545},
doi = {10.1117/12.863545},
issn = {0277-786X},
}TY - CONF
AU - Bormuth, Volker
AU - Varga, Vladimir
AU - Howard, Jonathon
AU - Schaeffer, Erik
PY - 2010
DA - 2010/01/01
TI - Breaking of bonds between a kinesin motor and microtubules causes protein friction
BT - OPTICAL TRAPPING AND OPTICAL MICROMANIPULATION VII
VL - 7762
IS - 776208
PB - SPIE-INT SOC OPTICAL ENGINEERING
SN - 0277-786X
AB - 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 fluctuation analysis con firmed 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.
DO - 10.1117/12.863545
UR - http://www.dx.doi.org/10.1117/12.863545
ER -