Abstract
Bacteriophage T7 gp4, a hexameric ring-shaped helicase, serves as a model protein for replicative helicases. T7 helicase couples dTTP hydrolysis to directional movement and DNA strand separation. Previous studies have shown that its DNA unwinding rate and dTTPase rate are sensitive to base pair (bp) stability.We confirm that the unwinding rate of T7 helicase decreases with increasing base pair (bp) stability. For duplexes containing > 35% GC basepairs, we observed stochastic pauses during unwinding.
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