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Volumn 12, Issue 18, 2011, Pages 2737-2739
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15N relaxation NMR studies of prolyl oligopeptidase, an 80 kDa enzyme, reveal a pre-existing equilibrium between different conformational states
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CIC BIOGUNE
(Spain)
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Author keywords
Ligand recognition; NMR spectroscopy; Prolyl oligopeptidase; Protein dynamics; Proteins
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Indexed keywords
NITROGEN 15;
PROLYL ENDOPEPTIDASE;
NITROGEN;
SERINE PROTEINASE;
ARTICLE;
CHEMICAL STRUCTURE;
CONFORMATIONAL TRANSITION;
HETERONUCLEAR SINGLE QUANTUM COHERENCE;
NUCLEAR MAGNETIC RESONANCE;
PRIORITY JOURNAL;
TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY;
ANIMAL;
CHEMISTRY;
PROTEIN CONFORMATION;
SWINE;
ANIMALS;
MODELS, MOLECULAR;
NITROGEN ISOTOPES;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PROTEIN CONFORMATION;
SERINE ENDOPEPTIDASES;
SWINE;
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EID: 83355160772
PISSN: 14394227
EISSN: 14397633
Source Type: Journal
DOI: 10.1002/cbic.201100614 Document Type: Article |
Times cited : (21)
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References (14)
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