Polyproline helices in protein structures: A statistical survey |
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Authors: | Berisio Rita Loguercio Salvatore De Simone Alfonso Zagari Adriana Vitagliano Luigi |
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Affiliation: | Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16. I-80134 Napoli, Italy. |
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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 beta-strands and coil regions and is similar to that of alpha-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 alpha-helices whereas they are fully non-correlated to propensities for beta-sheets. Finally, PPII propensities have been correlated with amino acid frequencies in structural proteins, such as collagen and extensins. |
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