Balance between asymmetry and abundance in multi-domain DNA-binding proteins may regulate the kinetics of their binding to DNA
Fig 3
Net charge of individual zinc-finger domains in tandem zinc-finger proteins.
The panels show the variation in normalized net charges for zinc finger proteins (ZFPs) comprising 3 (ZFP3) to 6 (ZFP6) zinc finger (ZF) domains. The number of domains is indicated by the superscript on ZFP in the title and the number of proteins shown in each group is indicated in the panel by a # mark. In each panel, three examples of proteins having asymmetric (purple) and symmetric (orange) electrostatics are shown. The normalized net charge of a ZF domain was obtained by subtracting the mean net charge of all the other ZF domains in that protein from the net charge of the ZF of interest.