A groundbreaking exploration of how sequence patterning, especially proline and charge distributions, governs the conformational behavior of intrinsically disordered regions (IDRs) even under multisite phosphorylation, with compensatory conformational changes maintaining overall dimensions.
Comprehensive 2016 Frontiers review on the diverse binding mechanisms of intrinsically disordered proteins (IDPs), covering theory, simulations, and experimental insights into how disorder facilitates interaction dynamics, specificity, and versatility in cellular signaling.
Comprehensive 2016 Frontiers review on the diverse binding mechanisms of intrinsically disordered proteins (IDPs), covering theory, simulations, and experimental insights into how disorder facilitates interaction dynamics, specificity, and versatility in cellular signaling.
Notes on 2010_PNAS study exploring how multisite phosphorylation of p53 modulates its interaction with CBP and transcriptional activation.
Notes on 2010_PNAS study exploring how multisite phosphorylation of p53 modulates its interaction with CBP and transcriptional activation.
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.
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.
Notes on the 2014 PNAS paper using single-molecule FRET to analyze the conformational response of intrinsically disordered proteins (IDPs) to molecular crowding. Highlights how IDP compaction depends not only on crowder concentration but also on crowder size, challenging traditional crowding models and introducing polymer-specific effects.
Notes on the 2014 PNAS paper using single-molecule FRET to analyze the conformational response of intrinsically disordered proteins (IDPs) to molecular crowding. Highlights how IDP compaction depends not only on crowder concentration but also on crowder size, challenging traditional crowding models and introducing polymer-specific effects.
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.
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.
Notes on the 2020 ACS paper introducing a combined experimental, computational, and analytical framework to study how IDRs respond to changes in chemical environments. The work reveals sequence-dependent compaction and expansion of IDRs under different solutes and highlights the role of chemical sensitivity as an added layer of regulation in biology.
Notes on the 2020 ACS paper introducing a combined experimental, computational, and analytical framework to study how IDRs respond to changes in chemical environments. The work reveals sequence-dependent compaction and expansion of IDRs under different solutes and highlights the role of chemical sensitivity as an added layer of regulation in biology.
Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
