Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 26, Pages 7564-7567Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201702626
Keywords
C-H center dot center dot center dot pi interactions; density functional calculations; J coupling; NMR spectroscopy; proteins
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Funding
- NSERC
- Banting Postdoctoral Fellowship
- Spedding Fellowship - Laboratory Directed Research and Development (LDRD) program at the Ames Laboratory
- US Department of Energy [DE-AC02-07CH11358]
- FRISBI [ANR-10-INSB-05-02]
- GRAL [ANR-10-LABX-49-01]
- European Research Council under the EU [260887]
- European Research Council (ERC) [260887] Funding Source: European Research Council (ERC)
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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 center dot center dot center dot pi hydrogenbond-like interactions involving the amide pi 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 center dot center dot center dot pi interaction adds a new dimension to the study of protein structure, function, and dynamics by NMR spectroscopy.
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