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Decoding Phase Separation of Prion-Like Domains through Data-Driven Scaling Laws - Abstract - Europe PMC

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PPRID: PPR675899 EMSID: EMS177635 bioRxiv preprint, version 1, posted 2023 June 14 https://doi.org/10.1101/2023.06.14.543914 Copyright notice This work is licensed under a CC BY-NC-ND 4.0 International license. This is an Open Access article, distributed under the terms of the Creative Commons Attribution licence (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted re-use, distribution, and reproduction in any medium, provided the original work is properly cited.. Proteins containing prion-like low complexity domains (PLDs) are common drivers of the formation of biomolecular condensates and are prone to misregulation due to amino acid mutations. Here, we exploit the accuracy of our residue-resolution coarse-grained model, Mpipi, to quantify the impact of amino acid mutations on the stability of an unprecedented set of 140 PLD mutants from six proteins (hnRNPA1, TDP43, FUS, EWSR1, RBM14, and TIA1). Our simulations reveal the existence of predictive rules that quant

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