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. 2019 Mar 26;9:5210. doi: 10.1038/s41598-019-41569-4

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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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AFM extension characteristics of utrophin terminal constructs. (a) Schematic of constructs analyzed by AFM. ABD - actin binding domain; DgBD - dystroglycan binding domain; SynBD - syntrophin binding domain; DBBD - dystrobrevin binding domain; NT - N-terminus; CR - cysteine rich domain; CT - C-terminus; ovals - spectrin-like repeats; diamonds - unstructured “hinge” regions. (b–d) Force vs extension representative trace curves for Utr NT-R10 (b), Utr R11-CT (c) and full-length utrophin (d). Approach – force on the cantilever as it approaches the substrate; Retract – force on the cantilever as the molecule is extended; Unfolding events – force minima corresponding to domain unfolding. WLC – worm like chain model fit to the force-extension behavior.