The diverse biological functions of intrinsically disordered proteins (IDPs) have markedly
raised our appreciation of protein conformational versatility, whereas the existence of …

Molecular dynamics simulations are a powerful theoretical tool to model the protein folding
process in atomistic details under realistic conditions. Combined with a number of …

Much of our understanding of folding mechanisms comes from interpretations of
experimental ϕ and ψ value analysis, relating the differences in stability of the transition …

The loss of conformational entropy is a major contribution in the thermodynamics of protein
folding. However, accurate determination of the quantity has proven challenging. We …

Although progress has been made to determine the native fold of a polypeptide from its
primary structure, the diversity of pathways that connect the unfolded and folded states has …

The burial of hydrophobic side chains in a protein core generally is thought to be the major
ingredient for stable, cooperative folding. Here, we show that, for the snow flea antifreeze …

Motivated by the relationship between the folding mechanism and the native structure, we
develop a unified approach for predicting folding pathways and tertiary structure using only …

A fundamental question in protein folding is whether the coil to globule collapse transition
occurs during the initial stages of folding (burst phase) or simultaneously with the protein …

Protein folding has been extensively studied, but many questions remain regarding the
mechanism. Characterizing early unstable intermediates and the high–free-energy transition …

The reliable folding of proteins is essential for their biological activities, while misfolding may
lead to severe diseases, such as Alzheimer's disease. However, our current knowledge of …