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 structual 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 1D and 2D spectra and the peptide solution conformation. The method appears particularly suited to obtaining information about the hydrogen bonding of backbone amide protons.

Niccolai, N., Bonci, A., Rustici, M., Scarselli, M., Neri, P., Esposito, G., et al. (1991). Nmr Delineation of Inner and Outer Protons From Paramagnetic Relaxation Perturbations In 1d and 2d Spectra of Peptides. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS II(9), 1453-1457 [10.1039/p29910001453].

Nmr Delineation of Inner and Outer Protons From Paramagnetic Relaxation Perturbations In 1d and 2d Spectra of Peptides

Niccolai, Neri;
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 structual 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 1D and 2D spectra and the peptide solution conformation. The method appears particularly suited to obtaining information about the hydrogen bonding of backbone amide protons.
1991
Niccolai, N., Bonci, A., Rustici, M., Scarselli, M., Neri, P., Esposito, G., et al. (1991). Nmr Delineation of Inner and Outer Protons From Paramagnetic Relaxation Perturbations In 1d and 2d Spectra of Peptides. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS II(9), 1453-1457 [10.1039/p29910001453].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/32052
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