The [Val3] analogue of the fungal tetrapeptide HC toxin has been synthesised. Conformational parameters of the peptide in solution have been measured by a variety of n.m.r. techniques. The 1H and 13C spectral features were assigned by using two-dimensional n.m.r. methods. Accurate backbone distances (proton-proton and proton-carbon) and those relative to the acceptors and donors of the hydrogen bonds were measured by using homo- and hetero-nuclear Overhauser effects and 1H and 13C relaxation parameters. The peptide conformation thus derived was identical with that of the parental toxin.
Mascagni, P., Prugnola, A., Gibbons, W.A., Niccolai, N. (1986). Synthesis and Solution Structure of [val3]-hc Toxin By H-1 and C-13 Nuclear-magnetic-resonance Relaxation Parameters. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS II, 7, 1015-1019 [10.1039/p29860001015].
Synthesis and Solution Structure of [val3]-hc Toxin By H-1 and C-13 Nuclear-magnetic-resonance Relaxation Parameters
Niccolai, Neri
1986-01-01
Abstract
The [Val3] analogue of the fungal tetrapeptide HC toxin has been synthesised. Conformational parameters of the peptide in solution have been measured by a variety of n.m.r. techniques. The 1H and 13C spectral features were assigned by using two-dimensional n.m.r. methods. Accurate backbone distances (proton-proton and proton-carbon) and those relative to the acceptors and donors of the hydrogen bonds were measured by using homo- and hetero-nuclear Overhauser effects and 1H and 13C relaxation parameters. The peptide conformation thus derived was identical with that of the parental toxin.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/33706
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