The cyclic decapeptide gramicidin S has been used as a model biopolymer to test the reliability of a strcutural method which is based on a relaxation analysis of heteronuclear selective NOEs. The observation of through-the-space dipolar couplings between intra- and inter residue amide protons and carbonyl carbons, perfectly consistent with the well established peptide solution conformation, confirms the effectiveness of this structural approach. As a corollary of the latter, carbonyl carbon resonances are unequivocally assigned. Moreover, a direct experimental proof of a Orn-NH2 → Phe CO hydrogen bonding is here given

Niccolai, N., Rossi, C., Mascagni, P., Neri, P., Gibbons, A.W. (1984). 1H-13C selective NOE studies of the decapeptide gramicidin S. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 124(3), 739-744 [10.1016/0006-291X(84)91020-9].

1H-13C selective NOE studies of the decapeptide gramicidin S

Niccolai, Neri;Rossi, Claudio;
1984-01-01

Abstract

The cyclic decapeptide gramicidin S has been used as a model biopolymer to test the reliability of a strcutural method which is based on a relaxation analysis of heteronuclear selective NOEs. The observation of through-the-space dipolar couplings between intra- and inter residue amide protons and carbonyl carbons, perfectly consistent with the well established peptide solution conformation, confirms the effectiveness of this structural approach. As a corollary of the latter, carbonyl carbon resonances are unequivocally assigned. Moreover, a direct experimental proof of a Orn-NH2 → Phe CO hydrogen bonding is here given
1984
Niccolai, N., Rossi, C., Mascagni, P., Neri, P., Gibbons, A.W. (1984). 1H-13C selective NOE studies of the decapeptide gramicidin S. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 124(3), 739-744 [10.1016/0006-291X(84)91020-9].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/9113
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