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. 2019 Jun 20;9:8836. doi: 10.1038/s41598-019-45237-5

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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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Establishing a high resolution (HR) targeted proteomics approach for low abundancy proteins. (A) Effect of different resolution on the mass separation and mass deviation. Right panel displays the resolution effect on a representative example of the PERK peptide GGFGVVFEAK transition y5, left panel shows the distribution of the average mass deviation at different resolution for all analyzed precursors. (B) Effect of different isolation widths on the mass accuracy and intensity at three different resolutions 15 k, 60 k and 240 k: Isolation width was set to m/z values of 0.4, 0.8 and 1.6, injection time to 500 ms and an AGC target value of 3 × 10⁶ was used for all measurements respectively. (C) Global effect of the injection time on the dot product at high resolution (upper panel), below representative example of injection time effects on ion traces of the PERK peptide GGFGVVFEAK at high resolution (240 k). All measurements were repeated at least 3 times.