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. Author manuscript; available in PMC: 2012 Sep 6.
Published in final edited form as: J Biol Chem. 2007 Dec 4;283(8):5118–5126. doi: 10.1074/jbc.M707548200

Fig. 6.

Fig. 6

Wild-type and truncated Hel308 helicase activity with a stalled replication fork model substrate

The activity of wild-type and K646-stop mutant of Hel308 were compared using a model substrate resembling a stalled replication fork. The black circle indicates the 5′-32P-labelled DNA end. Quantification of the reaction (right) shows that he truncated mutant (triangles) unwinds this substrate much faster than the wild-type protein (circles). The means of triplicate experiments are shown along with standard errors.

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