Does aqueous solvent discriminate among peptide conformers? To address this question,
we computed the solvation free energy of a blocked, 12‐residue polyalanyl‐peptide in …

In aqueous solution, the ensemble of conformations sampled by peptides and unfolded
proteins is largely determined by their interaction with water. It has been a long‐standing …

A significant fraction of the so‐called “random coil” residues in globular proteins exists in the
left‐handed poly (Pro) II conformation. In order to compare the behavior of this secondary …

Evidence from a variety of spectroscopic probes indicates that (ϕ, ψ) values corresponding
to the left-handed polyproline II helix (PII) are preferred for short alanine-based peptides in …

The finding that short alanine peptides possess a high fraction of polyproline II (PII) structure
(Φ=-75°, Ψ=+ 145°) at low temperature has broad implications for unfolded states of …

A simple approximation is developed to account for the dominant effects of solvation in
molecular dynamics simulations of biopolymers. A small number of water molecules are …

Recent studies have pointed out the important role of local water structures in protein
conformational stability. Here, we present an accurate and computationally effective way to …

While most force field efforts in biomolecular simulation have focused on the parametrization
of the protein, relatively little attention has been paid to the quality of the accompanying …

The 21 residue polyalanine-based Fs peptide was studied using thousands of long, explicit
solvent, atomistic molecular dynamics simulations that reached equilibrium at the ensemble …

Conformational ensembles of individual amino acid residues within model GxG peptides (x
representing different amino acid residues) are dominated by a mixture of polyproline II …