A new isotope-filtered experiment has been designed to measure homonuclear three-bond J(H(N)Halpha) coupling constants of unlabeled peptides complexed with labeled proteins. The new experiment is based on the 3D HNHA pulse scheme, and belongs to the 'quantitative J-correlation' type. It has been applied to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of human hepatitis C virus (HCV).
Cicero, D.o., Barbato, G., Koch, U., Ingallinella, P., Bianchi, E., Sambucini, S., et al. (2001). Measurement of homonuclear three-bond J(HNHa) coupling constants in unlabeled peptides complexed with labeled proteins: Application to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of hepatits C virus (HCV). JOURNAL OF BIOMOLECULAR NMR, 20, 23-29.
Measurement of homonuclear three-bond J(HNHa) coupling constants in unlabeled peptides complexed with labeled proteins: Application to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of hepatits C virus (HCV)
CICERO, DANIEL OSCAR;
2001-01-01
Abstract
A new isotope-filtered experiment has been designed to measure homonuclear three-bond J(H(N)Halpha) coupling constants of unlabeled peptides complexed with labeled proteins. The new experiment is based on the 3D HNHA pulse scheme, and belongs to the 'quantitative J-correlation' type. It has been applied to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of human hepatitis C virus (HCV).| File | Dimensione | Formato | |
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