ArticleProtein science : a publication of the Protein Society2014
Signatures of n→π* interactions in proteins.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Thioimidate Protection Enables Amide, Thioamide, and Amidine Installation at Aspartic Acid Residues.The Journal of organic chemistry · 2026Article
- The interplay between the pyramidalization of carbonyl carbons and the n → π* interactions in biomolecules.Protein science : a publication of the Protein Society · 2026Article
- Fragmentation Dynamics of Benzoyl Peroxide: Insights from Rotational Spectroscopy.The journal of physical chemistry letters · 2025Article
- Complementary Strategies for Installation of Thioimidates into Peptide Backbones.The Journal of organic chemistry · 2024Article
- Thioimidate Solutions to Thioamide Problems during Thionopeptide Deprotection.Organic letters · 2024Article
- Thioimidates provide general access to thioamide, amidine, and imidazolone peptide-bond isosteres.Methods in enzymology · 2024Article
- Enhanced Activity and Stability of an Acetyl Xylan Esterase in Hydrophilic Alcohols through Site-Directed Mutagenesis.Molecules (Basel, Switzerland) · 2023Article
- SM-COLSARSPROT: Highly Immunogenic Supramutational Synthetic Peptides Covering the World's Population.Frontiers in immunology · 2022Article
- Mapping of N-C Bond Formation from a Series of Crystalline Peri-Substituted Naphthalenes by Charge Density and Solid-State NMR Methodologies.Angewandte Chemie (International ed. in English) · 2021Article
- Hydrogen Bonds and n → π* Interactions in the Acetylation of Propranolol Catalyzed byACS omega · 2021Article
- Article
- Reconciling Electrostatic and n→π* Orbital Contributions in Carbonyl Interactions.Angewandte Chemie (International ed. in English) · 2020Article
- Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37-42) Peptide.Molecules (Basel, Switzerland) · 2020Article
- Observations of tetrel bonding between spChemical science · 2020Article
- Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone.Free radical biology & medicine · 2020Article
- Intermolecular Non-Covalent Carbon-Bonding Interactions with Methyl Groups: A CSD, PDB and DFT Study.Molecules (Basel, Switzerland) · 2019Article
- Secondary Forces in Protein Folding.ACS chemical biology · 2019Review
- Relative orientation of the carbonyl groups determines the nature of orbital interactions in carbonyl-carbonyl short contacts.Chemical science · 2019Article
- The n→π* Interaction.Accounts of chemical research · 2017Article
- Reciprocal carbonyl-carbonyl interactions in small molecules and proteins.Nature communications · 2017Article
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Authors and funding
5 authors.
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Abstract
The folding of proteins is directed by a variety of interactions, including hydrogen bonding, electrostatics, van der Waals' interactions, and the hydrophobic effect. We have argued previously that an n→π* interaction between carbonyl groups be added to this list. In an n→π* interaction, the lone pair (n) of one carbonyl oxygen overlaps with the π* antibonding orbital of another carbonyl group. The tendency of backbone carbonyl groups in proteins to engage in this interaction has consequences for the structures of folded proteins that we unveil herein. First, we employ density functional theory to demonstrate that the n→π* interaction causes the carbonyl carbon to deviate from planarity. Then, we detect this signature of the n→π* interaction in high-resolution structures of proteins. Finally, we demonstrate through natural population analysis that the n→π* interaction causes polarization of the electron density in carbonyl groups and detect that polarization in the electron density map of cholesterol oxidase, further validating the existence of n→π* interactions. We conclude that the n→π* interaction is operative in folded proteins.
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