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. 2018 Nov 20;8(2):e1532759. doi: 10.1080/2162402X.2018.1532759

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© 2018 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 2. — Biochemical characterization of affinity-enhanced TCR panels arising from the parental TCRs c672, c728 and c740.

Comparison of SPR data for affinity-enhanced TCR panels arising from three parental TCRs for which raw SPR data is shown in Figure S1. Note that TCR c753 is a version of c672 with the α-chain reverted fully to germline sequence, and that c753 therefore acted as the template for the daughter mutants c754-c756. Binding affinity analysis of the MAGE-A10_254-262-specific mutant TCR panels is illustrated in the upper panel, which shows the binding curve fits. K_D values shown in the bottom panel were obtained by equilibrium binding or kinetic analysis. From the c728 panel, c796-c799 were tested in a separate SPR experiment to c728 and c793-c795, leading to the difference in maximum binding levels.