The use of soluble spin labels to filter out the cross-peaks of outer proton nuclei in 2D NMR spectra is proposed as a general method of obtaining structural information about complex molecules. Gramicidin S, a decapeptide of well defined and stable structure, has been used as a model system to correlate the paramagnetic effects observed in 1 D and 2D spectra and the peptide solution conformation. The method appears particularly suited to obtaining information about the hydrogen bonding of backbone amide protons.
NMR Delineation of Inner and Outer Protons from Paramagnetic Relaxation Perturbations in 1D and 2D Spectra of Peptides
MOLINARI, Henriette
1991-01-01
Abstract
The use of soluble spin labels to filter out the cross-peaks of outer proton nuclei in 2D NMR spectra is proposed as a general method of obtaining structural information about complex molecules. Gramicidin S, a decapeptide of well defined and stable structure, has been used as a model system to correlate the paramagnetic effects observed in 1 D and 2D spectra and the peptide solution conformation. The method appears particularly suited to obtaining information about the hydrogen bonding of backbone amide protons.
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