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Institut de Recherche pour le Développement (IRD - France)
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Papers by Ed Oliver
Journal of the American Chemical Society, 1999
A novel isotopic labeling strategy is described for the structural analysis of proteins by NMR. O... more 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, C R , H R , C′) atoms leads to the formation of exclusively backbone-labeled protein. We demonstrate that the absence of the one bond scalar coupling between the 13 C R and 13 C atoms that is observed in uniformly 13 C 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 subunit of human chorionic gonadotropin isotopically enriched with 13 C (97%), 15 N (97%), and 2 H (50%) exclusively in the backbone atoms of Phe, Val, and Leu residues.
J Biomol Nmr, 2002
The implementation of [ 13 Cα, 13 C , 15 N, 2 Hα] labelled amino acids into proteins allows the a... more The implementation of [ 13 Cα, 13 C , 15 N, 2 Hα] labelled amino acids into proteins allows the acquisition of high resolution triple resonance experiments. We present for the first time resonance assignments facilitated by this new labelling strategy. The absence of 1 J Cα,Cβ couplings enables us to measure 1 J Cα,C scalar and 1 D Cα,C residual dipolar coupling constants using modified HNCA experiments which do not suffer from sensitivity losses characteristic for 13 C constant time experiments.
Journal of the American Chemical Society, 1999
A novel isotopic labeling strategy is described for the structural analysis of proteins by NMR. O... more 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, C R , H R , C′) atoms leads to the formation of exclusively backbone-labeled protein. We demonstrate that the absence of the one bond scalar coupling between the 13 C R and 13 C atoms that is observed in uniformly 13 C 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 subunit of human chorionic gonadotropin isotopically enriched with 13 C (97%), 15 N (97%), and 2 H (50%) exclusively in the backbone atoms of Phe, Val, and Leu residues.
J Biomol Nmr, 2002
The implementation of [ 13 Cα, 13 C , 15 N, 2 Hα] labelled amino acids into proteins allows the a... more The implementation of [ 13 Cα, 13 C , 15 N, 2 Hα] labelled amino acids into proteins allows the acquisition of high resolution triple resonance experiments. We present for the first time resonance assignments facilitated by this new labelling strategy. The absence of 1 J Cα,Cβ couplings enables us to measure 1 J Cα,C scalar and 1 D Cα,C residual dipolar coupling constants using modified HNCA experiments which do not suffer from sensitivity losses characteristic for 13 C constant time experiments.