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 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.
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 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.
