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. 2018 Mar 14;10(4):572–582. doi: 10.1080/19420862.2018.1442998

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© 2018 Amgen Inc, Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 4. — CID MS³ spectra of the disulfide-dissociated peptides TH3 (top) and TH11 peptides (bottom) within the V_H domain. Only one fragment ion was missing for both CID MS³ spectra of TH3 and TH11 to achieve an MS³ sequence coverage of 100%. Both C²² (H) and C⁹⁶ (H) residues were surrounded by fragment ions, and thus the location of disulfide linkages were unambiguously identified.