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. 2022 Oct 12;610(7933):796–803. doi: 10.1038/s41586-022-05314-8

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© The Author(s) 2022

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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Extended Data Fig. 2 — a, Proteins detected by MS, via their associated peptide fragments, are listed with their gene name and molecular mass. The number of identified unique peptides from both the native TMC-1 complex and from wild-type worms (C. elegans N2), used as a control, are also indicated. b, Amino acid sequence and secondary structure of C. elegans TMC-1 are shown. The secondary structure based on the cryo-EM structure is indicated above the sequences as cylinders (α-helices), black lines (loop regions), or dashed lines (disordered residues). Red lines above the sequences indicate C. elegans peptides found by MS. . Note that the TMC-1 segments, corresponding to the sequence of 13–33, 557–566, 567–587, 877–890, 897–904, 917–927, 972–996, 1041–1052, 1177–1190, 1192–1216, and 1261–1269 are also found by MS, but not indicated in b.