The cyclic decapeptide gramicidin S has been used as a model biopolymer to test the reliability of a structural 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., P., M., P., N., W. A., G. (1984). 1H-13C selective NOE studies of the decapeptide gramicidin S. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 124, 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 structural 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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/34124
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