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 …

The activity within a living cell is based on a complex network of interactions among
biomolecules, exchanging information and energy through biochemical processes. These …

We report a new algorithm for constructing pathways between local minima that involve a
large number of intervening transition states on the potential energy surface. A significant …

The last decade has witnessed a renewed interest in the coarse-grained (CG) models for
biopolymers, also stimulated by the needs of modern molecular biology, dealing with nano …

Impressive advances in the applications of bioinformatics for protein structure prediction
coupled with growing structural databases on one hand and the insurmountable time-scale …

The results of basin-hopping global optimization simulations are presented for four small, α-
helical proteins described by a coarse-grained potential. A step-taking scheme that …

We carry out a series of long atomistic molecular dynamics simulations to study the
unfolding of a small protein, chicken villin headpiece (HP-36), in water–ethanol (EtOH) …

Differential scanning calorimetry was used to measure the temperature dependence of the
absolute heat capacity of the 35-residue subdomain of the villin headpiece, a protein that …

Villin-type headpiece domains are approximately 70 amino acid modular motifs found at the
C terminus of a variety of actin cytoskeleton-associated proteins. The headpiece domain of …

Background Protein sequence evolution is constrained by the biophysics of folding and
function, causing interdependence between interacting sites in the sequence. However …