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. 2016 Dec 1;28(1):5–13. doi: 10.1007/s13361-016-1545-3

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© The Author(s) 2016

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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.

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Native MS compares well with alternative methods to probe quaternary structures. (a) Cartoon of the wild-type IgG4 antibody and an IgG4 antibody whereby the hinge region is deleted (IgG4Δhinge). IgG4Δhinge exists in solution in equilibrium between its monomeric (HL) and dimeric (HL₂) state. (b) Native MS of three HL mutants; IgG4Δhinge, R409KΔhinge, and F405QΔhinge. Two charge state distributions are observed for IgG4Δhinge corresponding to its monomeric and dimeric state, well separated in m/z space. In contrast, predominantly the monomeric and dimeric states were observed for the IgG4Δhinge variants F405Q and R409K, respectively. (c) Native PAGE of IgG4Δhinge, R409KΔhinge, and F405QΔhinge, showing different band migrations corresponding to the oligomeric status (i.e., monomeric/dimeric) of the variants in solution. (d) Size exclusion chromatography (SEC) multi-angle laser light scattering (MALLS) of IgG4Δhinge (red), R409KΔhinge (green), and F405QΔhinge (blue), showing the difference in retention times/molar masses measured reflecting their either monomeric, dimeric, or mixed status in solution [81]. The figure is adapted from [81]