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. 2019 Feb 21;10:891. doi: 10.1038/s41467-019-08869-9

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© The Author(s) 2019

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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Fig. 2 — Higher energy collisional dissociation (HCD) fragmentation spectra of GluC-digested CPS14-ComP bioconjugates. GluC-digested CPS14-ComP was subjected to HCD fragmentation enabling the confirmation of a single peptide attached to a glycan with the CPS14 repeating subunit. High collision energies (a) and low collision energies (b) regimens were undertaken to confirm the glycosylation of the peptide ₈₁ISASNATTNVATAT₉₄ with a 1378.47 Da glycan corresponding to HexNAc₂Hexose₆