Towards sequence-based principles for protein phase separation predictions |
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Institution: | 1. Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK;2. Department of Biomedical Sciences, University of Padova, PD 35131, Italy;3. Department of Physics and Astronomy, University of Padova, PD 35131, Italy |
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Abstract: | The phenomenon of protein phase separation, which underlies the formation of biomolecular condensates, has been associated with numerous cellular functions. Recent studies indicate that the amino acid sequences of most proteins may harbour not only the code for folding into the native state but also for condensing into the liquid-like droplet state and the solid-like amyloid state. Here we review the current understanding of the principles for sequence-based methods for predicting the propensity of proteins for phase separation. A guiding concept is that entropic contributions are generally more important to stabilise the droplet state than they are for the native and amyloid states. Although estimating these entropic contributions has proven difficult, we describe some progress that has been recently made in this direction. To conclude, we discuss the challenges ahead to extend sequence-based prediction methods of protein phase separation to include quantitative in vivo characterisations of this process. |
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Keywords: | Protein phase separation Sequence-based predictions Protein interactions Protein aggregation MBM"} {"#name":"keyword" "$":{"id":"pc_OpKHzW9eNS"} "$$":[{"#name":"text" "_":"multiplicity of binding modes |
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