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. 2016 Jun 22;6(6):160105. doi: 10.1098/rsob.160105

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© 2016 The Authors.

Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 3. — Thermal shift assay probing a panel of potential UspC ligands. (a) Bar graph illustrating shifts of T_m for a series of carbohydrates. Data shown are from three independent repeats. UspC_Nt mutants carrying a single alanine substitution at Asp145, Gln218 or Tyr292 are labelled as 145, 218 or 292, respectively. (b) Saturation binding curve derived from the thermal shift data varying the ligand concentration (0–200 mM). The apparent dissociation equilibrium constants K_d,app derived from these data by fitting a single-site saturation binding model are 27.7 ± 6.4 mM (d-glucosamine-6-phosphate) and 38.1 ± 3.5 mM (chitobiose).