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. 2019 Jun 20;9:8869. doi: 10.1038/s41598-019-45189-w

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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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Changes in overall α-helical content in ETR1 by tryptophan substitution. Secondary structure content of purified full-length ETR1 tryptophan mutants was determined by CD spectroscopy. Changes in α-helical content related to individual tryptophan mutants are shown as deviation from the tryptophan-free background mutant ETR1^W7X. All measurements were taken in triplicates. Mean and standard deviation are shown (*P ≤ 0.05; **P ≤ 0.02).