From exponentially large numbers of possible sequences, protein design seeks to identify
the properties of those that fold to predetermined structures and have targeted structural and …

Fast-folding proteins have been a major focus of computational and experimental study
because they are accessible to both techniques: they are small and fast enough to be …

The accuracy of atomistic physics-based force fields for the simulation of biological
macromolecules has typically been benchmarked experimentally using biophysical data …

Trp-cage is a designed 20-residue polypeptide that, in spite of its size, shares several
features with larger globular proteins. Although the system has been intensively investigated …

The Trp-cage, as the smallest miniprotein, remains the subject of numerous computational
and experimental studies of protein folding dynamics and pathways. The original Trp-cage …

We study the unbiased folding/unfolding thermodynamics of the Trp‐cage miniprotein using
detailed molecular dynamics simulations of an all‐atom model of the protein in explicit …

We attempt to understand the origin of enhanced stability in thermophilic proteins by
analyzing thermodynamic data for 116 proteins, the largest data set achieved to date. We …

Insights into the conformational passage of a polypeptide chain across its free energy
landscape have come from the judicious combination of experimental studies and computer …

Small proteins provide convenient models for computational studies of protein folding and
stability, which are usually compared with experimental data. Until recently, the unfolding of …

We simulate the folding/unfolding equilibrium of the 20-residue miniprotein Trp-cage. We
use replica exchange molecular dynamics simulations of the AMBER94 atomic detail model …