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. 2017 Aug 8;7:7540. doi: 10.1038/s41598-017-08021-x

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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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Characterization of HA mutant protein. (A) SEC-MALS analysis of the purified double mutant. The molecular masses of the CU44 wild-type and double mutant HA proteins agreed with the value of 67.2 kDa and 205.9 kDa, respectively, taking into account glycosylation. The flow rate in SEC-MALS was 0.5 ml/min using a UFLC system. (B) Differential scanning fluorimetry transition curves of the wild-type HA trimer (in black) and double mutant monomer (in red). Each HA protein was incubated at 25 °C for 30 sec, and then the temperature was increased by 0.5 °C every 30 sec for 50 min.