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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. 6 — Half-lives for PPIA-derived peptides in liver and cartilage, plotted as a function of mean squared error (of the model fit); calculated half-lives for PPIA are indicated by horizontal lines. The N-terminal peptide of PPIA with acetylation (green) exhibits a longer half-life than the non-acetylated form of the same peptide (red), in both liver and cartilage. Other peptides from PPIA (blue) do not contain the N-terminus and so may be from the modified or unmodified proteoform. The peptide half-life data are plotted as the best model fit to all observations of a given peptide ± the 2.5th and 97.5th percentile values from 200 simulations per peptide, based on a minimum of six peptide observations (of which at least three occurred at a single experimental timepoint), from a pool of n = 22 biologically independent samples. Source data are provided with this paper; raw mass spectrometry data are available as described in the “Data Availability” section.