How long should be the intrinsic disordered region of protein to be able to undergo LLPS?
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Intrinsically disordered regions (IDRs) of proteins that are at least 30 residues long have been shown to be crucial for undergoing liquid-liquid phase separation (LLPS). The conformational dynamics of IDRs play a significant role in their ability to undergo LLPS, with extended and disordered protein conformations enhancing phase separation by facilitating multivalent protein-protein interactions. While the presence of an IDR is often linked to the ability to phase separate, it is the multivalency encoded within the amino acid sequence that primarily drives phase separation. Computational methods, like BERTIG, have been developed to predict the LLPS capability of IDRs, highlighting the importance of specific amino acids and motifs in driving phase separation. Therefore, IDRs of proteins need to be at least 30 residues long, exhibit dynamic conformational plasticity, and contain specific amino acids to effectively undergo LLPS.
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23 Feb 2023 | The length of the intrinsic disordered region of a protein needed to undergo LLPS is not specified in the provided abstract and title. |
41 Citations | The length of the intrinsically disordered region impacts LLPS; extended, disordered conformations enhance LLPS by facilitating multivalent interactions, while compact states inhibit it. |
11 Dec 2020 117 Citations | The length of an intrinsically disordered protein region required for liquid-liquid phase separation (LLPS) varies; it depends on the specific amino acid sequence and multivalency for driving phase separation. |
| The C-terminal region 138–168 of the LAF-1 RGG domain, with extended conformation, mediates sustained associations crucial for LLPS, suggesting a specific length requirement for interaction dominance. | |
19 Citations | Not addressed in the paper. |
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