ArticleBiomolecules2022
Structural Achievability of an NH-π Interaction between Gln and Phe in a Crystal Structure of a Collagen-like Peptide.
Article in Biomolecules, 2022. 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, 12 citations in OpenAlex.
- Hidden Interactions: Quantum Perspectives in Drug Design.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide.Nature communications · 2025Article
- De Novo Design of Specific Heterotrimeric Collagen-Like Peptides via Genetic Algorithm.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- In Silico Design and Computational Elucidation of Hypothetical Resveratrol-Curcumin Hybrids as Potential Cancer Pathway Modulators.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Advances in nanotechnology-based approaches for the treatment of head and neck squamous cell carcinoma.RSC advances · 2024Review
- Stabilization of the retromer complex: Analysis of novel binding sites of bis-1,3-phenyl guanylhydrazone 2a to the VPS29/VPS35 interface.Computational and structural biotechnology journal · 2024Article
- Adaptation strategies of giant viruses to low-temperature marine ecosystems.The ISME journal · 2024Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NH-π interactions between polar and aromatic residues are well distributed in proteins whose stabilizing effects have been investigated in globular and fibrous proteins. In order to gain structural insights into side chain NH-π interactions, we solved a crystal structure of a collagen-like peptide containing Gln-Phe pairs. The Gln-Phe NH-π interactions were further characterized by quantum calculations, molecular simulations, and structural bioinformatics. The analyses indicated that the NH-π interactions are robust under various solvent conditions, can be distributed either on the protein surface or in its hydrophobic core and can form at a wide range of distances between residues. This study suggested that NH-π interactions can play a versatile role in protein design, including engineering hydrophobic cores, solvent accessible surfaces, and protein-protein interfaces.
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