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. 2021 Feb 5;12:828. doi: 10.1038/s41467-021-21063-0

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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. 2 — a, b Analytical ultracentrifugation analysis of the binding between yeast Hsp90 (Hsp82) and yeast p23 (Sba1) mutants. All measurements were performed in the presence of 2 mM AMP–PNP. Labeled p23 (p23*) was bound to Hsp90 and an excess of the depicted p23 mutants was added. c–e Isothermal titration calorimetry analysis of the affinity between yeast (c) p23^WT, (d) p23^Δ88 and (e) p23^W124A and yeast Hsp90 (Hsp82). The measurements were performed in the presence of AMP–PNP. The shown curves are representatives of at least two replicates.