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. 2024 Jul 10;31(12):1888–1897. doi: 10.1038/s41594-024-01355-x

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 4 — a, Relative deuterium uptake of DHFR peptides after 100 s exposure to deuterium. Values are the average of 2-4 replicates. Error bars represent s.d. See also Data S1. b, As in panel a, but showing relative deuterium uptake of DHFR peptides after 1000 s exposure to deuterium. c, Relative deuterium uptake of DHFR peptides after 10 s exposure to deuterium, as a percentage of the maximum possible exchange, for isolated DHFR (FL DHFR) and FL+50^stop. A maximally-deuterated control sample (FL+50^stop Max D) is shown as a reference. Data are presented as mean values of 2-4 replicates. Where shown, error bars represent SD, n = 3 or n = 4 independent experiments. d, As in panel c, but for 100 s exposure to deuterium. e, As in panel c, but for 1000 s exposure to deuterium. f, Representative mass spectra for peptide 9-28, charge state +2, after 10 s deuteration. See also Data S1.