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. 2021 Nov 26;12:6778. doi: 10.1038/s41467-021-26842-3

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© The Author(s) 2021

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. 7 — a Comparison of calculated peptide half-lives in cartilage, generated by ApplE Turnover and Turnover GUI. b Relative fractions of the three isotopic label combinations (Lys0Lys0, Lys0Lys8, Lys8Lys8) of missed cleavage peptides in cartilage, as a function of peptide half-life. The expected values for each experimental timepoint are plotted as solid curves; the observed data are matched-color open circles. Note that each of these missed cleavage plots is analogous to the single plot in Fig. 2b, which shows the relative fraction of unlabeled lysine (Lys0) for all peptides in cartilage. Results from other tissues are shown in Supplementary Figs. 7 and 8. Source data are provided with this paper; raw mass spectrometry data are available as described in the “Data Availability” section.