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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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Unique mechanical behavior of utrophin halves is maintained upon deletion of terminal domains. (a) Schematic of utrophin constructs lacking terminal domains and a 10-repeat construct spanning both N- and C-terminal halves. (b) Coomassie-stained gel of purified proteins (5ug) imaged on UVP GelDoc-It® Imaging System. (c) Circular dichroism melt curves of utrophin constructs measured at 1 °C intervals. Average melting temperatures ± standard deviation for Utr R1-10, R11-22,R1-22, and R6-15 are 45.7 ± 0.26 °C, 50.5 ± 0.3 °C, 47.0 ± 0.49 °C, and 45.4 ± 1.6, respectively. (d–f) Plots of probability distributions vs unfolding force of each unfolding event (N) for Utr R1-10 (d), Utr R11-22 (e), Utr R1-22 (f), and Utr R6-15 (g).