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.
