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Angew Chem Int Ed Engl. 2017 Jun 19;56(26):7564-7567. doi: 10.1002/anie.201702626. Epub 2017 May 22.

Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins.

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Department of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Street, Ottawa, Ontario, Canada.
Current address: US Department of Energy, Ames Laboratory, 213 Spedding Hall, Ames, IA, 50011, USA.
Université Grenoble Alpes, CNRS, CEAEA, Institut de Biologie Structurale (IBS), 71 Avenue des Martyrs, 38044, Grenoble, France.
Department of Biology, University of York, Wentworth Way, York, YO10 5DD, UK.


Protein structure and function is dependent on myriad noncovalent interactions. Direct detection and characterization of these weak interactions in large biomolecules, such as proteins, is experimentally challenging. Herein, we report the first observation and measurement of long-range "through-space" scalar couplings between methyl and backbone carbonyl groups in proteins. These J couplings are indicative of the presence of noncovalent C-H⋅⋅⋅π hydrogen-bond-like interactions involving the amide π network. Experimentally detected scalar couplings were corroborated by a natural bond orbital analysis, which revealed the orbital nature of the interaction and the origins of the through-space J couplings. The experimental observation of this type of CH⋅⋅⋅π interaction adds a new dimension to the study of protein structure, function, and dynamics by NMR spectroscopy.


C−H⋅⋅⋅π interactions; J coupling; NMR spectroscopy; density functional calculations; proteins

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