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Investigations on a flexible prolyl‐endopeptidase inhibitor in solution by NMR techniques
Author(s) -
Podányi Benjamin,
Bokotey Sándor,
Kánai Károly,
Fehér Miklós,
Hermecz István
Publication year - 1999
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/(sici)1097-458x(199905)37:5<346::aid-mrc466>3.0.co;2-w
Subject(s) - chemistry , conformational isomerism , vicinal , prolyl endopeptidase , proton nmr , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , molecule , proton , chemical shift , coupling constant , computational chemistry , organic chemistry , enzyme , physics , particle physics , quantum mechanics
4‐Phenylbutyrylprolylpyrrolidine, an inhibitor of prolyl‐endopeptidase, exists in solution as an equilibrium of trans and cis prolyl rotamers. The equilibrium ratio and the exchange rate of the rotamers were measured in several solvents. The conformational preferences of the flexible molecule were studied by NMR, based on proton–proton vicinal coupling constants, NOESY cross peak intensities and aromatic ring current shifts. Copyright © 1999 John Wiley & Sons, Ltd.