A conceptual leap in understanding protein folding, showing how water molecules and molecular chaperones act as weak, transient links that smooth energy landscapes and prevent conformational traps. This paper connects protein folding, dynamic networks, and game theory, offering a new way to see how folding and interaction landscapes are managed in crowded cellular environments.
A conceptual leap in understanding protein folding, showing how water molecules and molecular chaperones act as weak, transient links that smooth energy landscapes and prevent conformational traps. This paper connects protein folding, dynamic networks, and game theory, offering a new way to see how folding and interaction landscapes are managed in crowded cellular environments.
A modern view of allostery as an intrinsic property of protein dynamics, where conformational shifts, weak interactions, and energy landscapes enable regulation of function. Bridging classical models with cutting-edge experimental and theoretical insights, this review explores how proteins use dynamic ensembles and independent dynamic segments to facilitate signaling, folding, and ligand binding — redefining allostery beyond static views.
A modern view of allostery as an intrinsic property of protein dynamics, where conformational shifts, weak interactions, and energy landscapes enable regulation of function. Bridging classical models with cutting-edge experimental and theoretical insights, this review explores how proteins use dynamic ensembles and independent dynamic segments to facilitate signaling, folding, and ligand binding — redefining allostery beyond static views.
A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.
A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.
A 2010 Cell review expanding the classical models of protein-ligand binding to a dynamic landscape of conformational selection, induced fit, and independent dynamic segments. The paper highlights how ‘NOISE’—conformational fluctuations—can amplify signaling and regulate allosteric interactions, reshaping our understanding of binding and protein communication.
A 2010 Cell review expanding the classical models of protein-ligand binding to a dynamic landscape of conformational selection, induced fit, and independent dynamic segments. The paper highlights how ‘NOISE’—conformational fluctuations—can amplify signaling and regulate allosteric interactions, reshaping our understanding of binding and protein communication.
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 2024_ACS paper discussing the kinetic and structural principles of phosphorylation-driven protein switches and their biosensor applications.
Notes on 2024_ACS paper discussing the kinetic and structural principles of phosphorylation-driven protein switches and their biosensor applications.
Notes on 2004 Elsevier article discussing how weak links stabilize complex networks, with insights into phosphorylation, metabolic flux, and protein folding.
Notes on 2004 Elsevier article discussing how weak links stabilize complex networks, with insights into phosphorylation, metabolic flux, and protein folding.
Notes on 2010 Cell Review article exploring the structural and evolutionary principles that shape the dynamic regulatory mechanisms of protein kinases.
