Notes on 2008 Biophysical Journal paper analyzing the thermodynamics of membrane insertion for an H-ras lipopeptide anchor (ANCH), highlighting the role of enthalpy-driven hydrophobic effects and conformational selection.
Notes on 2008 Biophysical Journal paper analyzing the thermodynamics of membrane insertion for an H-ras lipopeptide anchor (ANCH), highlighting the role of enthalpy-driven hydrophobic effects and conformational selection.
Notes on 2000 Proteins paper introducing the concept of ’natively unfolded’ proteins and how charge and hydrophobicity dictate their intrinsic disorder under physiological conditions.
Notes on 2000 Proteins paper introducing the concept of ’natively unfolded’ proteins and how charge and hydrophobicity dictate their intrinsic disorder under physiological conditions.
Notes on 2013 PNAS paper introducing the role of charge distribution pattern (κ) in shaping IDP conformations. Highlights how linear charge segregation influences whether IDPs adopt random coil or compact, hairpin-like structures.
Notes on 2013 PNAS paper introducing the role of charge distribution pattern (κ) in shaping IDP conformations. Highlights how linear charge segregation influences whether IDPs adopt random coil or compact, hairpin-like structures.
Notes on 2010 PNAS paper exploring how net charge per residue (NCPR) governs the balance between collapsed and extended conformations in intrinsically disordered proteins (IDPs), with implications for understanding IDP behavior and function.
Notes on 2010 PNAS paper exploring how net charge per residue (NCPR) governs the balance between collapsed and extended conformations in intrinsically disordered proteins (IDPs), with implications for understanding IDP behavior and function.
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.
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.
Notes on 2002 APS paper analyzing the topology of potential energy landscapes, showing how minima and transition states form a static scale-free and small-world network. Offers insights into energy landscape organization, optimization, and system dynamics.
Notes on 2002 APS paper analyzing the topology of potential energy landscapes, showing how minima and transition states form a static scale-free and small-world network. Offers insights into energy landscape organization, optimization, and system dynamics.
Notes on 2005 Biophysical Journal article analyzing atomistic pathways of Ca²⁺ binding to calmodulin, highlighting stepwise binding, dehydration coupling, and residue dynamics.
Notes on 2005 Biophysical Journal article analyzing atomistic pathways of Ca²⁺ binding to calmodulin, highlighting stepwise binding, dehydration coupling, and residue dynamics.
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.
