Balance between asymmetry and abundance in multi-domain DNA-binding proteins may regulate the kinetics of their binding to DNA
Fig 2
Electrostatic properties of the C2H2-type zinc-finger proteins (ZFPs).
(A) The average number of positive (dark and light blue) and negative (red) charges are shown for human C2H2-type tandem ZFPs of different lengths (comprised of 3 (ZFP3) to 15 (ZFP15) zinc finger (ZF) domains. The His residue may be present in its positively charged (deep blue line) or neutral (light blue line) form. (B) The number of net charges on each zinc finger is shown for ZFP3–ZFP6. Each panel presents the analysis of five representative ZFPs (shown in five different colours) of the same length (as indicated by the superscript in the panel title). The analysis shows that the net charge of individual zinc finger domains within a protein can vary significantly.