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Solution structure of dynorphin A (1–17): a NMR study in a cryoprotective solvent mixture at 278 K

✍ Scribed by Roberta Spadaccini; Orlando Crescenzi; Delia Picone; Teodorico Tancredi; Piero Andrea Temussi

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 107 KB
Volume: 5
Category: Article
ISSN: 1075-2617
DOI: 10.1002/(sici)1099-1387(199907)5:7<306::aid-psc199>3.0.co;2-b

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✦ Synopsis

Dynorphin A, the endogenous agonist for the s 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 .

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