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. 2023 Feb 10;14:758. doi: 10.1038/s41467-023-36450-y

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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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Fig. 6 — a–c QCM-D binding assays analogous to Fig. 5, for Shh (a), Shh^K/A (b), and Shh^K/E (c), with an added step of competition with soluble heparin. d Overlays of frequency responses as shown in (a–c) demonstrate a reduced binding rate and increased unbinding rate in the wash buffer of Shh^K/E, and reduced unbinding of Shh^K/A and Shh^K/E upon competition with soluble heparin, compared to Shh. e Overlay of associated dissipation shifts as shown in (a–c) evidences reduced rigidification of the heparin layer by Shh^K/A, and even more so by Shh^K/E, compared to Shh, demonstrating that the second HS-binding site is essential for HS cross-linking. f Overlay of frequency responses (relative to full protein elution) from the start of soluble heparin-mediated protein elution (t = 0) until t = 40 min after elution start evidences an overall reduced elution rate for Shh^K/A and Shh^K/E compared to Shh, thus demonstrating that the second HS-binding site of Shh promotes rapid HS switching.