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. 2019 Feb 5;10:153. doi: 10.3389/fmicb.2019.00153

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Copyright © 2019 Zhao, Wu, Xu, Ma, Ding, Bai, Rong, Zhang, Li and Ji.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Sensorgram data of UreA-His and its mutants binding to Hsp60. (A–H) Wild-type UreA-His or its mutants with a series of concentrations (0.36, 0.73, 1.46, and 2.19 μM) were injected over a control surface (no Hsp60) and a surface containing ∼600 RU of Hsp60 for 120 s with the dissociation monitored for 800 s. Then, the analyte was removed by injecting 45 μl of 5 mM NaOH in 90 s to regenerate the surface. For the mutants, only three protein concentrations (0.73, 1.46, 2.19 μM) were retained in the graph. (I) Integrated sensorgram data of UreA-His and its seven mutants binding to Hsp60 with a concentration of 40 μg/ml (1.46 μM). All experiments were repeated at least three times.