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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
Published on: October 15, 2019
A motor that makes its own track: helicase unwinding of DNA
M D Betterton1, Frank Jülicher
1Insitut Curie, Physico-chimie Curie, UMR 168, 26 rue d'Ulm, 75248 Paris Cedex 05, France. mdb@colorado.edu
Abstract:
We study the unwinding of DNA by helicase proteins as a representative system in which a motor protein interacts with a mobile obstacle. In our discrete model, the interaction between the helicase and the DNA fork is characterized by an interaction potential. For the case of a hard-wall potential, the helicase opens the DNA by rectifying thermal fluctuations which spontaneously open base pairs. A potential with nonzero range describes the destabilization of the double strand by the enzymatic action of the helicase. We derive solutions for the opening speed as a function of the potential shape and relate our results to experiments on helicase motion.
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