The constrained backbone torsion angle of a proline (Pro) residue has usually been invoked
to explain its three-dimensional context in proteins. Here we show that specific interactions …

To study the influence of proline residues on three-dimensional structure, an analysis has
been made of all proline residues and their local conformations extracted from the …

Proline lacks an amide proton when found within proteins. This precludes hydrogen bonding
between it and hydrogen bond acceptors, and thus often restricts the residue to the first four …

The triple helical conformation observed in the collagen group of proteins is related to the
presence of large numbers of imino residues and is derived from the stereochemical …

In proteins, the proline ring exists predominantly in two discrete states. However, there is
also a small but significant amount of flexibility in the proline ring of high‐resolution protein …

The disrupting effect of a prolyl residue on an α‐helix has been analyzed by means of
conformational energy computations. In the preferred, nearly α‐helical conformations of Ac …

The well‐known preference of the peptide bond for the trans conformation has been
attributed to steric effects. Here, we show that a proline residue with an N‐formyl group (Hi …

Although hydrophobic interaction is the main contributing factor to the stability of the protein
fold, the specificity of the folding process depends on many directional interactions. An …

We examined CH/π hydrogen bonds in protein/ligand complexes involving at least one
proline residue using the ab initio fragment molecular orbital (FMO) method and the program …

The polyproline II (PPII) conformation of protein backbone is an important secondary
structure type. It is unusual in that, due to steric constraints, its main‐chain hydrogen‐bond …