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. 2010 Mar 9;38(8):2645–2662. doi: 10.1093/nar/gkq152

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Binding kinetics of interaction input devices. (A) Constitutive interaction between Leucine zippers E34 and R34 (proteins P21 and P22) at analyte concentrations from 22 to 1500 nM. (B) Rapamycin-induced interaction between FKBP12 and FRB(T2098L) (proteins P10 and P04) at analyte concentrations from 0.25 to 32 nM. SPR traces of binding and unbinding were fitted to a 1:1 interaction model (red line).