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. 2017 Aug 17;7:8648. doi: 10.1038/s41598-017-08917-8

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© The Author(s) 2017

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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Disaggregation reaction of aggregated EYFP tethered by a chaperone. (a) Schematic drawing of the construction of YFP-TB and YFP-TK_NBD-B are shown. (b) YFP-TB (left panel), YFP-TK_NBD-B (right panel), and their mutants (6.0 μM monomer) were heat treated at 80 °C for 15 min and the EYFP portions of these proteins were aggregated. The heat-treated fusion proteins were diluted to 0.3 μM monomer, incubated at 55 °C, and the fluorescence at 527 nm (excitation 513 nm) was monitored. After 2 min incubation, ATP (final concentration was 5 mM) was added and the fluorescence monitoring was continued. Fluorescence intensities are shown as a percentage of that prior to heat aggregation. (c) Initial rates of the recovery of the fluorescence were calculated from the measurements shown in (b). Error bars represent standard deviations of three or more independent measurements. WT, wild-type.