Abstract

A statistical survey of polyproline II (PPII) helices extracted from protein crystal structures is here reported. The average hydrophobicity of these helices is intermediate between those displayed by β-strands and coil regions and is similar to that of α-helices. PPII helices with amphipathic properties have been identified and classified. Amino acid propensities for PPII helices derived in this study differ significantly from those previously reported. They show a little albeit significant correlation with propensities for α-helices whereas they are fully non-correlated to propensities for β-sheets. Finally, PPII propensities have been correlated with amino acid frequencies in structural proteins, such as collagen and extensins.

Keywords: PPII helices, collagen, imino-acids, statistical survey, bioinformatics