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 …

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 the preceding paper, the structure of water around a model protein a-helix (made from
polyalanine) was investigated using two-dimensional projections of the molecular …

It has been suggested that denatured proteins are predisposed toward the left-handed
polyproline II (PII) conformation. One possible source of PII stability in the denatured state is …

In protein crystal structures, orderedwater molecules have been frequently observed at
instances where a-helices bend or fold. A series of molecular dynamics (MD) simulations …

The left‐handed polyproline II helix (PPII) is believed to be the preferred conformation for
proline‐rich regions of sequence in proteins. Such regions have been postulated to be …

Buried solvent molecules are common in the core of globular proteins and contribute to
structural stability. Folding necessitates the burial of polar backbone atoms in the protein …

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 …

The conformational properties of a β‐hairpin peptide (YITNSDGTWT) were studied by using
both explicit and implicit water simulations. The conformational space of the peptide was …

The main-chain conformations of 80 proteins were analyzed to identify helical structures that
commonly occur but do not fall into the known classes of α-helix, 3 10-helix and β-sheet. The …