| Literature DB >> 14754162 |
M D Betterton1, Frank Jülicher.
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.Entities:
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Year: 2003 PMID: 14754162 DOI: 10.1103/PhysRevLett.91.258103
Source DB: PubMed Journal: Phys Rev Lett ISSN: 0031-9007 Impact factor: 9.161