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ZB 10 - Soft Condensed Matter (R. Holyst)
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!

Publication

Small Crowders Slow Down Kinesin-1 Stepping by Hindering Motor Domain Diffusion

Author(s): Sozanski, Krzysztof and Ruhnow, Felix and Wisniewska, Agnieszka and Tabaka, Marcin and Diez, Stefan and Holyst, Robert
Title: Small Crowders Slow Down Kinesin-1 Stepping by Hindering Motor Domain Diffusion
Abstract: The dimeric motor protein kinesin-1 moves processively along against forces of up to 7 pN. However, the mechanism of generation is still debated. Here, we point to the crucial of diffusion of the tethered motor domain for the stepping of small crowders stop the motor at a viscosity of 5 to a hydrodynamic load in the sub-fN (similar to pN) range-whereas large crowders have no impact even at above 100 mPa.s. This indicates that the scale-dependent, viscosity experienced by the tethered motor domain is a key determining kinesin's functionality. Our results emphasize the of diffusion in the kinesin-1 stepping mechanism and the general importance of the viscosity scaling paradigm in nanomechanics.
Journal: PHYSICAL REVIEW LETTERS
Volume: 115
ID: ISI:000365003300012
Year: 2015
DOI: 10.1103/PhysRevLett.115.218102

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