Journal of Peptide Science· 2026Q2
Hydrogen Bonds Determining the Conformation of Isolated Amino Acid Residues in Proteins: Re‐Examination of the Fully Extended C5 Structures
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- Q2SCImago
- 2026year
Short summary
Intraresidue C5 hydrogen bonds stabilize fully extended amino acid conformations (φ, ψ ≈ ±180°) in proteins, with Gly showing the highest propensity and branched residues like Leu, Val, and Ile being disfavored.
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Key points
- Intraresidue C5 hydrogen bonds stabilize fully extended amino acid conformations (φ, ψ ≈ ±180°).
- Glycine has the highest propensity for C5 conformations, followed by Serine.
- Branched sidechain residues (Leu, Val, Ile) are strongly disfavored from adopting C5 conformations.
- Analysis used a high-resolution dataset of 6924 non-homologous x-ray diffraction structures (<1.6 Å resolution, <30% sequence identity).
AI-generated from the title and abstract; the full text is not read.
Abstract
Hydrogen bonds contribute substantially to the stabilisation of specific three-dimensional structures of peptides. The C5 hydrogen bond is an intraresidue interaction, which appears to contribute to the stabilisation of fully extended residue conformations, with backbone torsion angles (φ, ψ) lying close to ±180°. The present study revisits the occurrence of C5 conformations in proteins, using a high-resolution, non-homologous dataset of 6924 x-ray diffraction structures (sequence identity < 30%, resolution < 1.6 Å). Gly emerges as the residue with the highest propensity to adopt C5 conformations, followed by Ser. Residues with branched sidechains Leu, Val and Ile are strongly disfavoured. Specific examples in protein structures that have contiguous residues in C5 conformations are highlighted.
The authors' abstract, as published at the source. Journal of Peptide Science, 2026 · DOI ↗
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Physical and Theoretical ChemistryChemistry