A groundbreaking study connecting protein folding energy landscapes to functional conformational changes in signaling proteins, showing how transient, non-native hydrogen bonds lower transition barriers and facilitate activation without unfolding.
Notes on 2006_PNAS paper exploring conserved structural mechanisms of kinase activation via surface comparison.
Notes on a 2014 PNAS paper analyzing PKA dynamics through community analysis.
Notes on 2002 Cell review discussing conformational plasticity of protein kinases, highlighting key structural elements, activation mechanisms, and pseudosubstrate regulation. Includes insights on αC helix, activation loop, and therapeutic implications (e.g., Gleevec binding).
Notes on 2002 Cell review discussing conformational plasticity of protein kinases, highlighting key structural elements, activation mechanisms, and pseudosubstrate regulation. Includes insights on αC helix, activation loop, and therapeutic implications (e.g., Gleevec binding).
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 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 2017 Nature Communications paper revealing the 3D structure of the CaMKII holoenzyme in an activation-competent conformation, emphasizing the role of flexible linkers and dimeric kinase domain interactions in regulating activation and frequency decoding.
Notes on a 2017 Nature Communications paper revealing the 3D structure of the CaMKII holoenzyme in an activation-competent conformation, emphasizing the role of flexible linkers and dimeric kinase domain interactions in regulating activation and frequency decoding.
Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.
Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.
