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. 2010 Mar 3;107(14):6146–6151. doi: 10.1073/pnas.0912617107

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Fig. 3. — Light-induced interaction of His-tagged proteins followed by SPR. The association and dissociation kinetics of MBP-H₁₀ before (A) and after photoactivation (B) reveal a drastic change in affinity. Before photoactivation almost no interaction is observed, while after illumination His-tagged proteins are stably bound at high density. (C) Protein binding to the PA tris-NTA-His₅ surface (30 min after dissociation) are plotted against the concentration of MBP-H₆ and MBP-H₁₀ before (open) and after (closed symbols) photoactivation. (D) Comparison of the relative binding signals obtained for MBP-H₆ and MBP-H₁₀ (625 nM each) interacting with different PA tris-NTAs. The relative amounts of bound proteins (30 min after dissociation) are shown before (gray) and after photoactivation (red) in comparison to the binding observed with nonactivatable tris-NTA. Maximum binding of MBP-H_6/10 after photoactivation for each interface is normalized to 100%.