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. 2021 Apr 21;12:2360. doi: 10.1038/s41467-021-22634-x

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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. 1 — A Schematic of a VWF monomer, marked above with binding sites of related proteins, is aligned with various AIM-A1 fragments. NAIM and CAIM are colored cyan and orange, respectively. B Schematic of single-molecule optical tweezer apparatus in this study. The 1272–1458 disulfide bond is marked red in the A1 domain. C Representative force-extension traces of AIM-A1 (black), NAIM-A1 (cyan), and A1-CAIM (orange). The extension event in each trace is marked by an arrowhead. D Plots of unfolding force versus unfolding extension for noted AIM-A1 fragments and fits to the worm-like chain model. Force data are presented as mean values ± standard deviation, and extension data are presented as the peak of the Gaussian fit ± the full width at half maximum (FWHM) of Gaussian fit divided by the square root of counts. The data was obtained from n = 52, 80, and 75 biologically independent single-molecule tethers for AIM-A1, NAIM-A1 and A1-CAIM, respectively. E Plots of unfolding force versus loading rate for noted AIM-A1 fragments and fits to the Bell–Evans model. Unfolding force data are presented as the center of the tallest bin of the histogram ± one-half of the bin width. The data were obtained from n = 52, 80, and 75 biologically independent single-molecule tethers for AIM-A1, NAIM-A1, and A1-CAIM, respectively. F Average occurrence of a single long unfolding event (black bar), two short unfolding events (gray bar), and a single short unfolding event (white bar) during repeated cycles of extension and retraction. The constructs were pulled at 200 nm/s after relaxation under 1 pN for 1 s. Error bars represent standard deviation. N = 12, 17, and 19 biologically independent single-molecule tethers for AIM-A1, NAIM-A1, and A1-CAIM, respectively. Source data for (D–F) are provided in three worksheets of the Source Data file.