lundi 18 septembre 2023 11:00
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Intrinsically disordered proteins (IDPs) lack rigid structure, being instead endowed with a high degree of flexibility. In the last two decades, the involvement of IDPs in a plethora of cellular functions has been recognised, including the process of liquid-liquid phase separation (LLPS), which leads to the formation of biomolecular condensates also known as membrane-less organelles. In an extreme form of pleiotropism, it appears possible that a single IDP can perform multiple functions by profoundly altering its solubility, degree of compactness, and ability to form liquid condensates or insoluble, hyperstructured aggregates, as in the case of amyloid fibrils.
This complex and contradictory behaviour of IDPs is largely conferred by their composition, characterised by a high frequency of charged residues, proline and glycine, and a relatively low percentage of hydrophobic and aromatic residues, which typically form the ‘hydrophobic core’ of classically structured proteins.
Recent works highlighting the role of the abundance of charged residues and their ‘patterning’ distribution on conformational and functional aspects of IDPs will be illustrated, often achieved through the rational design of charge permutants.
Publié le septembre 1, 2023