Constantly advancing computer simulations of biomolecules provide huge amounts of data
that are difficult to interpret. In particular, obtaining insights into functional aspects of …

Using enhanced-sampling replica exchange fully atomistic molecular dynamics simulations,
we show that, individually, urea and guanidinium chloride (GdmCl) denature the Trpcage …

The use of computers for predicting the structures and properties of biomolecules has
closely paralleled computer development since the 1950s, and has been one of the core …

Mechanically driven unfolding is a useful computational tool for extracting the energetics
and stretching pathway of peptides. In this work, two representative β-hairpin peptides …

Glycosylation is one of the most common post-translational modifications (PTMs), which
provides a large proteome diversity. Previous work on glycosylation of globular proteins has …

Six mutants of the tryptophan zipper peptide trpzip1 have been computationally and
experimentally characterized. We determine the varying roles in secondary structure stability …

The binding of therapeutics to human serum albumin (HSA), which is an abundant protein in
plasma poses a major challenge in drug discovery. Although HSA has several binding …

Assemblies of proteins and charged macromolecules (polyelectrolytes) find important
applications as pharmaceutical formulations, biocatalysts, and cell-contacting substrates. A …

Studying a set of helix-folding polyalanine peptides with systematically inserted chiral
inversions in explicit water, we investigate quantitatively the effect of chiral perturbations on …

Understanding how proteins fold has remained a problem of great interest in biophysical
research. Atomistic computer simulations using physics-based force fields can provide …