Until now it has been impractical to observe protein folding in silico for proteins larger than
50 residues. Limitations of both force field accuracy and computational efficiency make the …

High-accuracy ab initio folding has remained an elusive objective despite decades of effort.
To explore the folding landscape of villin headpiece subdomain HP35, we conducted two …

The 35-residue subdomain of the villin headpiece (HP35) is a small ultrafast folding protein
that is being intensely studied by experiments, theory, and simulations. We have solved the …

We report the modification and parametrization of the united-residue (UNRES) force field for
energy-based protein structure prediction and protein folding simulations. We tested the …

Parametrization and testing of a new all-atom force field for organic molecules and peptides
with fixed bond lengths and bond angles are described. The van der Waals parameters for …

A major difficulty in experimental studies of protein folding is the lack of nonperturbing,
residue specific probes of folding. Here, we demonstrate the ability to resolve protein folding …

We report the development of internal coordinate mechanics force field (ICMFF), new force
field parameterized using a combination of experimental data for crystals of small molecules …

In the last decades biomolecular simulation has made tremendous inroads to help elucidate
biomolecular processes in-silico. Despite enormous advances in molecular dynamics …

Equilibrium Fourier transform infrared (FTIR) and temperature-jump (T-jump) IR
spectroscopic techniques were used to study the thermodynamics and kinetics of the …

The carboxylate side chains of Asp and Glu have significant coupling with the amide states
of the backbone of the Villin headpiece. In two-dimensional spectroscopy, cross peaks are …