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. 2021 Feb 19;12:1185. doi: 10.1038/s41467-021-21352-8

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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. 3 — a Mass-to-charge vs. collisional cross section distribution of all peptides in this study colored by the GRAVY hydrophobicity index (n = 559,979). b Subset of peptides with C-terminal arginine or lysine colored by the fraction of prolines in the linear sequence (n = 452,592). c Histidine-containing peptides of (b) colored by the relative position of histidine (n = 171,429). Trend lines (dashed) are fitted to the overall peptide distribution to visualize the correlation of ion mass and mobility in each charge state.