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Protein Science (2001), 10:2627-2632.
Copyright © 2001 The Protein Society

FOR THE RECORD

Preferred proline puckerings in cis andtrans peptide groups: Implications for collagen stability

Luigi Vitagliano1, Rita Berisio1, Antonio Mastrangelo2, Lelio Mazzarella1,2,3 and Adriana Zagari1,2,3

1 Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy
2 Dipartimento di Chimica, Università degli Studi di Napoli "Federico II", I-80126 Napoli, Italy
3 CEINGE, Biotecnologie avanzate Scarl, Napoli, Italy

Reprint requests to: Luigi Vitagliano, Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 6, I-80134, Napoli, Italy; e-mail: luigiv{at}chemistry.unina.it; fax: 39-0812536603.

The interplay between side-chain and main-chain conformations is a distinctive characteristic of proline residues. Here we report the results of a statistical analysis of proline conformations using a large protein database. In particular, we found that proline residues with the preceding peptide bond in the cis state preferentially adopt a down puckering. Indeed, out of 178 cis proline residues, as many as 145 (81%) are down. By analyzing the 1–4 and 1–5 nonbonding distances between backbone atoms, we provide a structural explanation for the observed trend. The observed correlation between proline puckering and peptide bond conformation suggests a new mechanism to explain the reported shift of the cis-trans equilibrium in proline derivatives. The implications of these results for the current models of collagen stability are also discussed.

Keywords: Proline; cis peptide; hydroxyproline; statistical analysis; collagen

Abbreviations: cisPro and transPro, proline residues with the peptide bond of the preceding residue in the cis and trans conformations, respectively • upPro and downPro, proline residues with up and down side-chain puckerings, respectively • 4R-Hyp, 4R-hydroxyproline • 4S-Hyp, 4S-hydroxyproline • 4R-Flp, 4R-fluoroproline • 4S-Flp, 4S-fluoroproline


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Copyright © 2001 by The Protein Society.