ArticleThe journal of physical chemistry. B2024
Aromatic Residues in Proteins: Re-Evaluating the Geometry and Energetics of π-π, Cation-π, and CH-π Interactions.
Article in The journal of physical chemistry. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed.
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- Molecular determinants of arginine versus lysine cation-π interactions in biomolecular condensates.Communications chemistry · 2026Article
- Dual-functional self-assembled nanosystems with enhanced protease resistance: Promoting bacterial aggregation and immune activation for multidrug-resistant bacterial infection.Asian journal of pharmaceutical sciences · 2026Article
- Stereospecific Assembly of Triply Chiral Pseudopeptidic Cages Through Dynamic Dual Chirality Transfer.Angewandte Chemie (International ed. in English) · 2026Article
- Peptide-based ligand antagonists block a Vibrio cholerae adhesin.FEBS letters · 2026Article
- Exploring FDA-approved small molecules for their potential as PD-1/PD-L1 inhibitors: integrating computational screening with experimental testing.Journal of molecular modeling · 2026Article
- Structure-Based Virtual Screening of Plant-Derived Flavonoids as Putative GLUT9 Binders with Antioxidant Properties.Molecules (Basel, Switzerland) · 2026Article
- Recent Advances in Bioconjugation of Aromatic Amino Acid Residues by a Reactivity-Guided Approach.Chemical record (New York, N.Y.) · 2026Review
- The Molecular Basis of Growth Control in Guanine Crystals.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Influence of Dimerization on Aromaticity in Benzene and Heteroaromatic Rings.The Journal of organic chemistry · 2026Article
- Hidden Interactions: Quantum Perspectives in Drug Design.Methods in molecular biology (Clifton, N.J.) · 2026Review
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- Active Site Residues Contribute to the Multistep Dynamics of Dicyclotyrosine Bound to CYP121A1 ofBiochemistry · 2025Article
- Solution structure of the Sox2 DNA-binding domain reveals conformational selection in DNA binding.Nucleic acids research · 2025Article
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- Making Sense of Heteroatom Effects in π-π Interactions.Journal of the American Chemical Society · 2025Article
- PInteract: Detecting Aromatic-Involving Motifs in Proteins and Protein-Nucleic Acid Complexes.Biomolecules · 2025Article
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2 authors.
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Abstract
Aromatic residues can participate in various biomolecular interactions, such as π-π, cation-π, and CH-π interactions, which are essential for protein structure and function. Here, we re-evaluate the geometry and energetics of these interactions using quantum mechanical (QM) calculations, focusing on pairwise interactions involving the aromatic amino acids Phe, Tyr, and Trp and the cationic amino acids Arg and Lys. Our findings reveal that π-π interactions, while energetically favorable, are less abundant in structured proteins than commonly assumed and are often overshadowed by previously underappreciated, yet prevalent, CH-π interactions. Cation-π interactions, particularly those involving Arg, show strong binding energies and a specific geometric preference toward stacked conformations, despite the global QM minimum, suggesting that a rather perpendicular T-shape conformation should be more favorable. Our results support a more nuanced understanding of protein stabilization via interactions involving aromatic residues. On the one hand, our results challenge the traditional emphasis on π-π interactions in structured proteins by showing that CH-π and cation-π interactions contribute significantly to their structure. On the other hand, π-π interactions appear to be key stabilizers in solvated regions and thus may be particularly important to the stabilization of intrinsically disordered proteins.
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