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. 2021 Mar 2;11:4976. doi: 10.1038/s41598-021-83771-3

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Modelling of the MAPRE2 N68S mutation. (a, b) The size and hydrophobicity difference between (a) wild type (Asn) and (b) mutant (Ser) residue makes the mutant unable to form the same hydrogen bonds. (c) Aggregation propensity prediction TANGO scores per residue for wild type MAPRE2. Vertical red line indicates the position of N68. (d) Model structure of MAPRE2 with the strong APR colored in red. (e) Energetic landscape of the mechanism proposed. N68S mutation is indicated in red and wild type energy landscape in grey. N68S thermodynamically destabilizes and kinetically slows down the folding reaction, resulting in higher energies for N and T^N⇋U and less natively folded protein (N native fold, U unfolded state, A aggregated state, T transition state).