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. 2019 Feb 14;9:2050. doi: 10.1038/s41598-018-35535-9

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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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Schematic of the principle of donor quenching for protein interaction affinity determination by FRET assay. (A) Diagram of fluorescence emissions of FRET pair, CyPet and YPet, when tagged with interactive partners, SUMO1 and Ubc9, respectively. The fluorescence emission of donor CyPet-SUMO1 decreases when it binds acceptor Ypet-Ubc9. (B) Quantitative analysis of fluorescence signals. The decrease of CyPet emission is proportional the concentration of bound donor/acceptor complex.