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. 2018 Mar 2;8:3955. doi: 10.1038/s41598-018-22199-8

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Dynamic and thermodynamic behavior of different glycoforms of IgG-Fc. (a) The peptide where each glycoform of IgG-Fc produced differences in deuterium uptake is depicted in magenta. The terminal galactose units are depicted with yellow sticks. (b) Sequence of the peptide of IgG-Fc showing differential deuterium exchange rates. (c) Relative deuterium uptake for each glycoform. (d) Representation of the van’t Hoff plot corresponding to the binding of each glycoform to a surface decorated with Mut FcγRIIIa. Temperature dependence of the dissociation constant K_D yields the van’t Hoff enthalpy (ΔH°), entropy (−TΔS°) and free energy (ΔG°). (e) Comparison of the values of the thermodynamic parameters determined from panel d.