Polyproline Helices in Protein Structures: A Statistical Survey

Title: Polyproline Helices in Protein Structures: A Statistical Survey

Volume: 13 Issue: 8

Author(s): Rita Berisio, Salvatore Loguercio, Alfonso De Simone, Adriana Zagari and Luigi Vitagliano

Affiliation:

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

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.

Cite this article as:

Berisio Rita, Loguercio Salvatore, De Simone Alfonso, Zagari Adriana and Vitagliano Luigi, Polyproline Helices in Protein Structures: A Statistical Survey, Protein & Peptide Letters 2006; 13 (8) . https://dx.doi.org/10.2174/092986606777841154