The use of soluble spin labels to filter out the cross peaks of outer proton nuclei in 2D NMR spectra has been proposed as a general method to obtain structural information for complex molecules. Here the paramagnetic effects observed on backbone protons of an unfolded 27 amino acid peptide are discussed. The lack of any differential intensity change of the NH-Halpha cross-peaks in TOCSY spectra is suggested as an additional general criterion for the identification of unfolded structures.
Esposito, G., Molinari, H., Pegna, M., Niccolai, N., Zetta, L. (1993). A H-1-nmr Study On the Interaction of Aminoxyl Paramagnetic Probes With Unfolded Peptides. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS II(8), 1531-1534 [10.1039/p29930001531].
A H-1-nmr Study On the Interaction of Aminoxyl Paramagnetic Probes With Unfolded Peptides
Niccolai, Neri;
1993-01-01
Abstract
The use of soluble spin labels to filter out the cross peaks of outer proton nuclei in 2D NMR spectra has been proposed as a general method to obtain structural information for complex molecules. Here the paramagnetic effects observed on backbone protons of an unfolded 27 amino acid peptide are discussed. The lack of any differential intensity change of the NH-Halpha cross-peaks in TOCSY spectra is suggested as an additional general criterion for the identification of unfolded structures.
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https://hdl.handle.net/11365/35172
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