We propose a phase coexistence based mechanism for activity of helicases, ubiquitous enzymes that unwind double stranded DNA. The helicase–DNA complex constitutes a fixed-stretch ensemble that entails the coexistence of domains of zipped and unzipped phases of DNA, separated by a domain wall. The motor action of the helicase leads to a change in the position of the fixed constraint thereby shifting the domain wall on dsDNA. We associate this off-equilibrium domain wall motion with the unzipping activity of the helicase. We show that this proposal gives a clear and consistent explanation of the main observed features of helicases.
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Bhattacharjee et al. (2003) studied this question.
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