Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability(753 views) Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
Keywords: Cis Peptide, Collagen, Hydroxyproline, Statistical Analysis, Isoprotein, Article, Isomer, Isomerism, Priority Journal, Protein Conformation, Protein Stability, Structure Activity Relation, Algorithms, Models, Molecular, Protein Binding,
Affiliations: *** IBB - CNR ***
Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, I-80126 Napoli, Italy
CEINGE, Biotecnologie Avanzate Scarl, Napoli, Italy
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Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability
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.
Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability
No results.
Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability
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