The mechanism of protein folding (represented schematically below) is one of the most
fascinating problems in the field of chemical reactions. This review presents the progess …

Many small, monomeric proteins fold with simple two-state kinetics and show wide variation
in folding rates, from microseconds to seconds. Thus, stable intermediates are not a …

Recent experimental results suggest that the native fold, or topology, plays a primary role in
determining the structure of the transition state ensemble, at least for small, fast-folding …

An implementation of classical molecular dynamics on parallel computers of increased
efficiency has enabled a simulation of protein folding with explicit representation of water for …

The interplay between structure-search of the native structure and desolvation in protein
folding has been explored using a minimalist model. These results support a folding …

This paper surveys the emerging role of statistical mechanics and polymer theory in protein
folding. In the polymer perspective, the folding code is more a solvation code than a code of …

Experimental and theoretical studies together are providing insights into the mechanism by
which proteins fold. Our present knowledge of the essential aspects of the folding reaction is …

▪ Abstract This review describes how kinetic experiments using techniques with dramatically
improved time resolution have contributed to understanding mechanisms in protein folding …

Many small proteins seem to fold by a simple process explicable by conventional chemical
kinetics and transition-state theory. This assumes an instant equilibrium between reactants …

A change in the perception of the protein folding problem has taken place recently. The
nature of the change is outlined and the reasons for it are presented. An essential element is …