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 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 …

Despite proline being assumed to be a helix-breaker, a large number of α-helices are found
to contain Pro in globular as well as membrane proteins. Proline has no free NH group and …

In this report we describe a general survey of all helices found in 57 of the known protein
crystal structures, together with a detailed analysis of 48 α-helices found in 16 of the …

Crystal structure analysis of proline‐containing α‐helices in proteins has been carried out.
High resolution crystal structures were selected from the Protein Data Bank. Apart from the …

Free‐energy simulations have been used to estimate the change in the conformational
stability of short polyalanine α‐helices when one of the alanines is replaced by a proline …

A survey of 322 proteins showed that the short polar (SP) side chains of four residues, Thr,
Ser, Asp, and Asn, have a very strong tendency to form hydrogen bonds with neighboring …

The amino acid sequence and chemical interactions at the ends of 163 helices were
surveyed so as better to understand amino acid preferences previously observed …

We describe a novel N-terminal α-helix local motif that involves three hydrophobic residues
and a Pro residue (Pro-box motif). Database analysis shows that when Pro is the N-cap of …

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 …