The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

In the last years polyproline II (PPII) structure has been demonstrated to be essential to
biological activities such as signal transduction, transcription, cell motility, and immune …

A sequence of seven alanine residues—too short to form an α-helix and whose side chains
do not interact with each other—is a particularly simple model for testing the common …

The first crystal structure of an oligoproline adopting an all-trans polyproline II (PPII) helix is
presented. The high-resolution structure provides detailed insight into the dimensions and …

The left‐handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is
remarkably similar to that of unfolded proteins. This similarity has been used as the basis for …

The importance of the left-handed polyproline II (PPII) helical conformation has recently
become apparent. This conformation generally is involved in two important functions …

We compare the conformational distributions of Ace‐Ala‐Nme and Ace‐Gly‐Nme sampled
in long simulations with several molecular mechanics (MM) force fields and with a fast …

Classical descriptions of the three‐dimensional shapes of proteins usually invoke three
main structures: α‐helix, β‐sheet, and β‐turn. More recently, the polyproline II (PPII) structure …

During the late maturation stage of seed development, water content decreases greatly. One
of the most striking characteristics of mature orthodox seeds is their ability to withstand …

Polypeptide sequences encoding the single exons of human tropoelastin were synthesized
and their conformations were studied in different solvents and at different temperatures by …