ArticleJournal of computational chemistry2019
Hydrogen bond donors and acceptors are generally depolarized in α-helices as revealed by a molecular tailoring approach.
Article in Journal of computational chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Exploring Substituted Tetrazoloquinazoline: Biological Activities, Molecular Docking Analysis, and Anti-Breast Cancer MCF7/HER2 Effects.Advances in pharmacological and pharmaceutical sciences · 2024Article
- Quantum chemical studies on hydrogen bonds in helical secondary structures.Biophysical reviews · 2022Review
- Some reflections on a career in science and a note of thanks to the contributors of this Special Issue.Biophysical reviews · 2022Article
- Depolarizing Effects in Hydrogen Bond Energy in 3International journal of molecular sciences · 2022Article
- Molecular Structure-Based Screening of the Constituents ofCurrent issues in molecular biology · 2022Article
- Hydrogen bond donors and acceptors are generally depolarized in α-helices as revealed by a molecular tailoring approach.Journal of computational chemistry · 2019Article
- Studies on Molecular Dynamics of Intrinsically Disordered Proteins and Their Fuzzy Complexes: A Mini-Review.Computational and structural biotechnology journal · 2019Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogen-bond (H-bond) interaction energies in α-helices of short alanine peptides were systematically examined by precise density functional theory calculations, followed by a molecular tailoring approach. The contribution of each H-bond interaction in α-helices was estimated in detail from the entire conformation energies, and the results were compared with those in the minimal H-bond models, in which only H-bond donors and acceptors exist with the capping methyl groups. The former interaction energies were always significantly weaker than the latter energies, when the same geometries of the H-bond donors and acceptors were applied. The chemical origin of this phenomenon was investigated by analyzing the differences among the electronic structures of the local peptide backbones of the α-helices and those of the minimal H-bond models. Consequently, we found that the reduced H-bond energy originated from the depolarizations of both the H-bond donor and acceptor groups, due to the repulsive interactions with the neighboring polar peptide groups in the α-helix backbone. The classical force fields provide similar H-bond energies to those in the minimal H-bond models, which ignore the current depolarization effect, and thus they overestimate the actual H-bond energies in α-helices. © 2019 The Authors. Journal of Computational Chemistry published by Wiley Periodicals, Inc.
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