Intrinsically Disordered Regions Are Poised to Act as Sensors of Cellular Chemistry

Notes on the 2023 TIBS review proposing that intrinsically disordered regions (IDRs), with their sequence-dependent structural biases, are well-suited to act as sensors and actuators of cellular physicochemistry. Discusses physical principles, molecular mechanisms, and experimental strategies for investigating IDR sensitivity and highlights their potential biological roles.

Structural Biases in Disordered Proteins Are Prevalent in the Cell

Notes on the 2024 Nature paper exploring how sequence-dependent structural biases in intrinsically disordered proteins (IDPs) are preserved inside cells and how they respond to environmental changes. Using a combination of FRET, SAXS, SEC, and simulations, the study establishes glycine-serine repeats as model-free standards and demonstrates that IDP ensembles encode functional biases persistent in cellular contexts.

Structural Biases in Disordered Proteins Are Prevalent in the Cell

Notes on the 2024 Nature paper exploring how sequence-dependent structural biases in intrinsically disordered proteins (IDPs) are preserved inside cells and how they respond to environmental changes. Using a combination of FRET, SAXS, SEC, and simulations, the study establishes glycine-serine repeats as model-free standards and demonstrates that IDP ensembles encode functional biases persistent in cellular contexts.

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