The protein folding problem was first articulated as question of how order arose from
disorder in proteins: How did the various native structures of proteins arise from interatomic …

Protein folding should be complex. Proteins organize themselves into specific three-
dimensional structures, through a myriad of conformational changes. The classical view of …

The recent availability of long equilibrium simulations of protein folding in atomistic detail for
more than 10 proteins allows us to identify the key interactions driving folding. We find that …

We have developed a computer algorithm, FOLDEF (for FOLD-X energy function), to provide
a fast and quantitative estimation of the importance of the interactions contributing to the …

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 …

Protein folding and binding are kindred processes. Many proteins in the cell are unfolded, so
folding and function are coupled. This paper investigates how binding kinetics is influenced …

How fast can a protein possibly fold? This question has stimulated experimentalists to seek
fast folding proteins and to engineer them to fold even faster. Proteins folding at or near the …

A complete understanding of a protein-folding mechanism requires description of the
distribution of microscopic pathways that connect the folded and unfolded states. This …

Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

Biomolecules are the prime information processing elements of living matter. Most of these
inanimate systems are polymers that compute their own structures and dynamics using as …