Proline/sidechain C-H/O interactions stabilize <i>cis</i>-proline.

ABSTRACT: Bioinformatics analysis was conducted on proteins in the PDB to identify local structures that can stabilize the cis-proline conformation. C-H/O interactions were observed between a sidechain oxygen and Pro C-Hα in the cis-proline conformation at Glu-Pro, Asp-Pro, Gln-Pro, Asn-Pro, Ser-Pro, and Thr-Pro sequences. These C-H/O interactions are apparently most stabilizing at Glu-Pro sequences, which have a substantially higher than average frequency of cis-proline (7.1% of all Glu-Pro amide bonds in the PDB). DFT calculations were conducted to understand the bases and geometries of C-H/O interactions in these sequences. Computationally, these residues all exhibit close C-H/O interactions (substantially below the 2.72 Å sum of the van der Waals radii of H and O), with the

SUBMITTER: Oven HC 

PROVIDER: S-EPMC12862571 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature