Peptide bonds revisited.

ABSTRACT: Understanding the structural and chemical properties of peptide bonds within protein secondary structures is vital for elucidating their roles in protein folding, stability and function. This study examines the distinct characteristics of peptide bonds in α-helices and β-strands using a nonredundant data set comprising 1024 high-resolution protein crystal structures from the Protein Data Bank (PDB). The analysis reveals surprising and intriguing insights into bond lengths, angles, dihedral angles, electron-density distributions and hydrogen bonding within α-helices and β-strands. While the respective bond lengths (CN and CO) do not differ much between helices and strands, the bond angles (∠CNC_α and ∠OCN) are significantly larger in strands compared with helices. Furthermore, the

SUBMITTER: Panjikar S 

PROVIDER: S-EPMC12044857 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature