Conformational preferences of amino acid residues in water are determined by the
backbone and side-chain properties. Alanine is known for its high polyproline II (pPII) …

Molecular dynamics (MD) simulations have been used to determine the two dimensional
free energy surface of the alanine dipeptide in solution. The intramolecular dipeptide …

The structure and dynamics of the water hydrating peptides and proteins are examined here
at atomic resolution via molecular dynamics simulations. Detailed solvation density and …

New experimental techniques are capable of determining the relative population of
conformations adopted by short alanine peptides in water. Most of the existing all-atom force …

A 100 ns molecular dynamics simulation of penta‐alanine in explicit water is performed to
study the reversible folding and unfolding of the peptide. Employing a standard principal …

We have combined neutron solution scattering experiments with molecular dynamics
simulation to isolate an excess experimental signal that is caused solely by N-acetyl-leucine …

We have carried out molecular dynamics simulations to study the conformational equilibria
of two blocked dipeptides, Ac-Ala-Ala-NHMe and trans-Ac-Pro-Ala-NHMe, in water (Ac …

Conventional molecular dynamics simulations on 50 ns to 1 μs time scales were used to
study the effects of explicit solvent models on the conformational behavior and solvation of …

We have carried out conformational energy calculations on alanine-based copolymers with
the sequence Ac-AAAAAXAAAA-NH2 in water, where X stands for lysine or glutamine, to …

The free energy landscapes of peptide conformations in water have been observed by the
enhanced conformational sampling method, applying the selectively enhanced …