Journal
NATURE CHEMISTRY
Volume 2, Issue 6, Pages 466-471Publisher
NATURE PORTFOLIO
DOI: 10.1038/NCHEM.650
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Funding
- L'Association pour la Recherche sur le Cancer
- EU [FP7-PEOPLE-IRG-2008]
- Agence Nationale de la Recherche
- Human Frontiers Science Programme
- Centre National de la Recherche Scientifique
- Natural Sciences and Engineering Research Council of Canada
- High-Performance Virtual Computing Laboratory
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XH/pi interactions make important contributions to biomolecular structure and function. These weakly polar interactions, involving pi-system acceptor groups, are usually identified from the three-dimensional structures of proteins. Here, nuclear magnetic resonance spectroscopy has been used to directly detect methyl/pi (Me/pi) interactions in proteins at atomic resolution. Density functional theory calculations predict the existence of weak scalar (J) couplings between nuclei involved in Me/pi interactions. Using an optimized isotope-labelling strategy, these J couplings have been detected in proteins using nuclear magnetic resonance spectroscopy. The resulting spectra provide direct experimental evidence of Me/pi interactions in proteins and allow a simple and unambiguous assignment of donor and acceptor groups. The use of nuclear magnetic resonance spectroscopy is an elegant way to identify and experimentally characterize Me/pi interactions in proteins without the need for arbitrary geometric descriptions or pre-existing three-dimensional structures.
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