Quantum chemical studies on hydrogen bonds in helical secondary structures.

ABSTRACT: We present a brief review of our recent computational studies of hydrogen bonds (H-bonds) in helical secondary structures of proteins, α-helix and 3₁₀-helix, using a Negative Fragmentation Approach with density functional theory. We found that the depolarized electronic structures of the carbonyl oxygen of the ith residue and the amide hydrogen of the (i + 4)th residue cause weaker H-bond in an α-helix than in an isolated H-bond. Our calculations showed that the H-bond energies in the 3₁₀-helix were also weaker than those of the isolated H-bonds. In the 3₁₀-helices, the adjacent N-H group at the (i + 1)th residue was closer to the C=O group of the H-bond pair than the adjacent C=O group in the 3₁₀-helices, whereas the adjacen

SUBMITTER: Takano Y 

PROVIDER: S-EPMC9842822 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature