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Exploring the molecular grammar of IDP assembly and condensation at ultra-high throughput

CORDIS · observation · Publication date unknown

nted breakthroughs in protein structural biology, with the resolution revolution in cryo-electron microscopy and the release of AlphaFold. The combination of advanced experimental structural biology, machine learning algorithms and molecular simulations has put the fully quantitative description of how the structure and interactions of folded proteins are defined by their amino acid sequence within close reach. This leaves us with a final frontier in protein science, namely to achieve a similar level of understanding for intrinsically disordered proteins (IDPs). The energy landscapes of IDPs often comprise a multitude of nearly isoenergetic states, that include assembled forms, such as amyloid fibrils and liquid condensate droplets. Much effort has been spent in order to achieve an understanding of the molecular grammar of IDP assembly and condensation, i.e. how amino acid sequence defines both kinetics and thermodynamics of these processes. Current state of the art is to evaluate a few dozens of sequence perturbations quantitatively in vitro. In EMMA, I propose to develop a fundame

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award

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SIGNED

region

EU

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1995554

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EUR