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. © 2006 Bentham Science Publishers Ltd.
Polyproline helices in protein structures: A statistical survey / Berisio, R.; Loguercio, S.; De Simone, A.; Zagari, A.; Vitagliano, L.. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - 13:8(2006), pp. 847-854. [10.2174/092986606777841154]
Polyproline helices in protein structures: A statistical survey
De Simone A.;Zagari A.;
2006
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. © 2006 Bentham Science Publishers Ltd.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
