Journal
PROTEIN SCIENCE
Volume 10, Issue 12, Pages 2627-2632Publisher
COLD SPRING HARBOR LAB PRESS
DOI: 10.1110/ps.ps.26601a
Keywords
proline; cis peptide; hydroxyproline; statistical analysis; collagen
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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.
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