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. 2019 Jun 24;10:2775. doi: 10.1038/s41467-019-10696-x

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© The Author(s) 2019

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. 3 — The OaAEP1-dependent polyprotein immobilization verified by single-molecule AFM. a The schematic shows that OaAEP1 facilitates a covalent anchoring of (poly)protein on a glass surface as well as a specifically probing by an XDoc-functionalized AFM tip. b Representative curves of (Ub)_n in the specific attachment showed a high detachment force from the Coh-XDoc interaction and more unfolding peaks. c, d The statistical analysis of the (Ub)_n indicated the number of curves with a specific number of ubiquitin peaks. Most curves showed the number of Ub unfolding peaks between three and six (>90%). e The scatter plot shows the relationship between unfolding/rupture force and ΔLc for (Ub)_n, Xmodule of the XDoc (ΔLc = 35 nm), and the CBM. f The overlay of all curves with CBM unfolding first show the complete unfolding of the polyprotein (Ub)₆ using the OaAEP1-dependent polyprotein immobilization method (n = 52). The covalent immobilization with a high detachment force enables the complete unfolding of all subdomains in the polyprotein. Source data of Fig. 3e are provided as a Source Data file