Format

Send to

Choose Destination
Nat Chem. 2010 Jun;2(6):466-71. doi: 10.1038/nchem.650. Epub 2010 May 2.

Direct detection of CH/pi interactions in proteins.

Author information

1
CEA, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France. michael.plevin@ibs.fr

Abstract

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.

PMID:
20489715
DOI:
10.1038/nchem.650
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center