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 …

Transmembrane segments (TM) are important structural elements that often define the
functional domain of membrane proteins.'. 2 Structural studies of TM segments are thus …

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 …

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 …

Amino acids in peptides and proteins display distinct preferences for α-helical, β-strand, and
other conformational states. Various physicochemical reasons for these preferences have …

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 …

Hydration of the 16-residue β-hairpin fragment of the 2GB1 protein in the folded and
unfolded ensembles is studied with mTIP3P and TIP4P solvent models using the …

Transmembrane (TM) segments of integral membrane proteins are putatively α‐helical in
conformation, yet their primary sequences are rich in residues known in globular proteins as …

Recent work has shown that the nature of hydration of pure hydrophobic surfaces changes
with the length scale considered: water hydrogen-bonding networks adapt to small exposed …

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 …