Infrared (IR) spectroscopy has been widely utilized for the study of protein folding, unfolding,
and misfolding processes. We have previously developed a theoretical method for …

The LYS24/29NLE double mutant of villin headpiece subdomain (HP35) is the fastest
folding protein known so far with a folding time constant of 0.6 μ s⁠. In this work, the folding …

A physics-based method aimed at determining protein structures by using NOE-derived
distances together with observed and computed 13C chemical shifts is proposed. The …

The 36-residue helical subdomain of the villin headpiece, HP36, is one of the smallest
cooperatively folded proteins, folding on the microsecond time scale. The domain is an …

Successful ab initio folding of proteins with both α-helix and β-sheet requires a delicate
balance among a variety of forces in the simulation model, which may explain that the …

We determined the potentials of mean force corresponding to the bending of virtual-bond
angles (θ) for use in our united-residue (UNRES) force field. The potentials were determined …

The efficient expression of small to midsize polypeptides and small marginally stable
proteins can be difficult. A new protein fusion system is developed to allow the expression of …

The villin headpiece subdomain (HP36) is a widely used system for protein-folding studies.
Nuclear magnetic resonance cross-correlated relaxation rates arising from correlated …

We present an extension of the all-atom internal-coordinate force field, ICMFF, that allows for
simulation of heterogeneous systems including hexopyranose saccharides and glycan …

This paper proposes the Protein Ensemble Method (PEM) to model equilibrium fluctuations
in proteins where fragments of the protein polypeptide chain can move independently of one …