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. 2014 Jan 15;4(1):130090. doi: 10.1098/rsob.130090

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© 2014 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 6. — KRT10-TRD is bound in two contiguous paperclip-associated binding sites within BR_187–385. (a) The location of each substituted residue is indicated. The centre of mass of each residue is displayed as a sphere and coloured according to its importance for binding to KRT10-TRD (red and blue for low and high binding intensities, respectively). The introduced substitutions did not significantly alter the overall secondary structure of the mutated BR_187–385 proteins (see electronic supplementary material, figure S7). (b) Normalized intensity values were determined for binding of WT BR_187–385 and each mutated variant to KRT10-TRD coated in wells of ELISA plates. Values are given as mean with standard deviation. WT and mutated BR_187–385 variants were classified into groups a–d using the Tukey test at a significance level of p < 0.05.