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. 2015 Feb 13;5(1):121–141. doi: 10.3390/biom5010121

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Thermodynamic binding properties for the interaction of protein variants on the AGT-LRM background with Pex5p-pbd. (A) Free energy (ΔG), enthalpy (ΔH) and entropy (−TΔS) contributions to the binding reaction; (B,C) Thermodynamic dissection of binding enthalpies (B) and heat capacity changes (ΔC_p, C) into their intrinsic contribution (estimated from polar and apolar ΔASA using the crystal structure for the complex; Figure 1) and the contribution from conformational changes. In (A,B), data are mean ± s.d. for three independent experiments at 25 °C.