Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3969
Title: A H-1-nmr Study On the Interaction of Aminoxyl Paramagnetic Probes With Unfolded Peptides
Authors: G., Esposito
H., Molinari
M., Pegna
Niccolai, Neri 
L., Zetta
Issue Date: 1993
Project: None 
Journal: JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS II
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.
Description: 
47493
URI: http://hdl.handle.net/20.500.12779/3969
ISSN: 0300-9580
DOI: 10.1039/p29930001531
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