A 1H NMR study on the interaction of aminoxyl paramagnetic probes with unfolded peptides

Gennaro Esposito; Henriette Molinari; Monica Pegna; Neri Niccolai; Lucia Zetta

doi:10.1039/p29930001531

A ¹H NMR study on the interaction of aminoxyl paramagnetic probes with unfolded peptides

Gennaro Esposito, Henriette Molinari, Monica Pegna, Neri Niccolai, Lucia Zetta

Chemistry

Research output: Contribution to journal › Article › peer-review

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-Hα cross-peaks in TOCSY spectra is suggested as an additional general criterion for the identification of unfolded structures.

Original language	English (US)
Pages (from-to)	1531-1534
Number of pages	4
Journal	Journal of the Chemical Society, Perkin Transactions 2
Issue number	8
DOIs	https://doi.org/10.1039/p29930001531
State	Published - 1993

ASJC Scopus subject areas

General Chemistry

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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-Hα cross-peaks in TOCSY spectra is suggested as an additional general criterion for the identification of unfolded structures.",

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AU - Molinari, Henriette

AU - Pegna, Monica

AU - Niccolai, Neri

AU - Zetta, Lucia

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A ¹H NMR study on the interaction of aminoxyl paramagnetic probes with unfolded peptides

Abstract

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