title: 15N relaxation NMR studies of prolyl oligopeptidase, an 80 kDa enzyme, reveal a pre-existing equilibrium between different conformational states.
abstract: Open and closed: The characterization of protein mobility is crucial for the understanding of biological functions. We have applied NMR spectroscopy to study the conformational dynamics of the 80 kDa enzyme prolyl oligopeptidase (POP). Our results revealed that POP is highly dynamic and that inhibition of catalytic activity shifts this conformational equilibrium towards a less dynamic state.
authors: Institute for Research in Biomedicine, Baldiri Reixac 10, 08028 Barcelona, Spain.
authors: Nessim
authors: N
authors: Kichik
authors: Teresa
authors: T
authors: Tarragó
authors: Birgit
authors: B
authors: Claasen
authors: Margarida
authors: M
authors: Gairí
authors: Oscar
authors: O
authors: Millet
authors: Ernest
authors: E
authors: Giralt
mesh_terms: D000818:Animals; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D000085822:Prolyl Oligopeptidases; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry*; D013552:Swine
chemical_list: D009587:Nitrogen Isotopes; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases