Dynorphin A the endogenous agonist for the kappa opioid receptor, has been studied by NMR spectroscopy in methanol, acetonitrile, DMSO and in mixtures of hexafluaroacetone/water and DMSO/water. NMR data in the DMSO/water cryomixture at 278 K are consistent with a conformer in which the N-terminal part, like the corresponding message domain of enkephalins, is poorly ordered, whereas the C-terminal part is folded in a loop centred around Pro(10). The folded structure of the C-terminal part [address moiety] may shed light on the role of the essential residues Arg(7), Lys(11) and Lys(13). Copyright (C) 1999 European Peptide Society and John Wiley & Sons, Ltd.
Solution structure of dynorphin A (1-17): a NMR study in a cryoprotective solvent mixture at 278 K / R., Spadaccini; Crescenzi, Orlando; Picone, Delia; T., Tancredi; Temussi, PIERO ANDREA. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - STAMPA. - 5:7(1999), pp. 306-312. [10.1002/(SICI)1099-1387(199907)5:7<306]
Solution structure of dynorphin A (1-17): a NMR study in a cryoprotective solvent mixture at 278 K
CRESCENZI, ORLANDO;PICONE, DELIA;TEMUSSI, PIERO ANDREA
1999
Abstract
Dynorphin A the endogenous agonist for the kappa opioid receptor, has been studied by NMR spectroscopy in methanol, acetonitrile, DMSO and in mixtures of hexafluaroacetone/water and DMSO/water. NMR data in the DMSO/water cryomixture at 278 K are consistent with a conformer in which the N-terminal part, like the corresponding message domain of enkephalins, is poorly ordered, whereas the C-terminal part is folded in a loop centred around Pro(10). The folded structure of the C-terminal part [address moiety] may shed light on the role of the essential residues Arg(7), Lys(11) and Lys(13). Copyright (C) 1999 European Peptide Society and John Wiley & Sons, Ltd.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.