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Solution structure of dynorphin A (1–17): a NMR study in a cryoprotective solvent mixture at 278 K 1
Author(s) -
Spadaccini Roberta,
Crescenzi Orlando,
Picone Delia,
Tancredi Teodorico,
Temussi Piero Andrea
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199907)5:7<306::aid-psc199>3.0.co;2-b
Subject(s) - dynorphin , chemistry , moiety , acetonitrile , nuclear magnetic resonance spectroscopy , κ opioid receptor , solvent , agonist , stereochemistry , proton nmr , organic chemistry , opioid peptide , receptor , biochemistry , opioid
Dynorphin A, the endogenous agonist for the κ opioid receptor, has been studied by NMR spectroscopy in methanol, acetonitrile, DMSO and in mixtures of hexafluoroacetone/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 © 1999 European Peptide Society and John Wiley & Sons, Ltd.