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. 2013 Aug 19;41(21):9812–9824. doi: 10.1093/nar/gkt734

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© The Author(s) 2013. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Binding kinetics to the canonical site. DNA-binding kinetics of WT KpnI and the mutants was assayed by SPR spectroscopy. Biotinylated oligonucleotide harboring the canonical (-GGTACC-) site was immobilized onto a streptavidin chip. The proteins were passed over the DNA with restricted flow rates to measure the association and dissociation rates, as described in ‘Materials and Methods’ section. (A) Sensorgrams of WT, D16N, D148E and D16N/D148E. Graphical representation of the association (B) and dissociation (C) rates of the proteins is shown.