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. 2019 Nov 7;9:16162. doi: 10.1038/s41598-019-52121-9

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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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Comparison of model (grey) and crystal structure (red) of the fusion to helix 2 of the dArmRP. (a) Superposition of model (grey) and crystal structure (red, 1.6 Å resolution) of an N-terminal DARPin-dArmRP fusion. N- and C-termini of the proteins are marked. The fusion of DARPin D12 was made to H3 of a dArmRP with four internal repeats, with a shared helix length of 5 amino acids. The close-up view shows the distortion of the first helix of the DARPin. (b) Detailed view of the changed interface between model and experimental structure. The left picture is showing the model, the right one the structure in which Tyr150 inserts into the interface between the shared helix and the DARPin.