López Asamar, AbrahamHerranz-Trillo, F.Kotev, MartinGairí Tahull, MargaridaGuallar, VictorBernadó Peretó, PauMillet Aguilar-Galindo, ÒscarTarragó Clua, Maria TeresaGiralt Lledó, Ernest2018-10-152018-10-1520161439-4227https://hdl.handle.net/2445/125313Deciphering conformational dynamics is crucial for understanding the biological functions of proteins and for designing compounds targeting them. In particular, providing an accurate description of microsecond-millisecond motions opens the opportunity for regulating protein-protein interactions (PPIs) by modulating the dynamics of one interacting partner. Here we analyzed the conformational dynamics of prolyl oligopeptidase (POP) and the effects of active-site-directed inhibitors on the dynamics. We used an integrated structural biology approach based on NMR spectroscopy and SAXS experiments complemented by MD simulations. We found that POP is in a slow equilibrium in solution between open and closed conformations, and that inhibitors effectively abolished this equilibrium by stabilizing the enzyme in the closed conformation.5 p.application/pdfeng(c) Wiley-VCH, 2016Espectroscòpia de ressonància magnètica nuclearProteïnesNuclear magnetic resonance spectroscopyProteinsinfo:eu-repo/semantics/article6620302018-10-15info:eu-repo/semantics/openAccess26918396