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. 2023 Feb 9;30(3):383–390. doi: 10.1038/s41594-022-00913-5

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© The Author(s) 2023

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. 7 — Indicated CLPs (12–22 μM) were heated in the absence of peptide (black curves), in the presence of 500 μM FG peptide (blue curves) or in the presence of 500 μM GG peptide (orange curves). The FG peptide induced a clear shift in the melting profile of WT CLPs (upper left panel), thus indicating binding. In all other cases, the melting curves are virtually superimposable with their respective no-peptide controls, indicating lack of binding.

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