Browse by author
Lookup NU author(s): Professor Steve Homans
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
A novel isotopic labeling strategy is described for the structural analysis of proteins by NMR. Overexpression of a protein in a mammalian cell-line cultured in a medium containing amino acids labeled only in the backbone (N, Cα, Hα, C‘) atoms leads to the formation of exclusively backbone-labeled protein. We demonstrate that the absence of the one bond scalar coupling between the 13Cα and 13Cβ atoms that is observed in uniformly 13C enriched proteins offers a substantial sensitivity and resolution advantage in triple resonance NMR experiments that are commonly used to obtain backbone resonance assignments. This approach is illustrated in application to the β subunit of human chorionic gonadotropin isotopically enriched with 13C (97%), 15N (97%), and 2H (50%) exclusively in the backbone atoms of Phe, Val, and Leu residues.
Author(s): Coughlin PE, Anderson FE, Oliver EJ, Brown JM, Homans SW, Pollak S, Lustbader JW
Publication type: Article
Publication status: Published
Journal: Journal of the American Chemical Society
Year: 1999
Volume: 121
Issue: 50
Pages: 11871-11874
Print publication date: 04/12/1999
ISSN (print): 0002-7863
ISSN (electronic): 1520-5126
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/ja993083w
DOI: 10.1021/ja993083w
Altmetrics provided by Altmetric
