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Free keywords:
Magic-angle spinning solid-state NMR; Relax-EXSY; H/D exchange; Deuteration; Amide protons; Proton detection; PrgI; Relaxation
Abstract:
In this report we present site-specific measurements of amide hydrogen-deuterium exchange rates in a protein in the solid state phase by MAS NMR. Employing perdeuteration, proton detection and a high external magnetic field we could adopt the highly efficient Relax-EXSY protocol previously developed for liquid state NMR. According to this method, we measured the contribution of hydrogen exchange on apparent N-15 longitudinal relaxation rates in samples with differing D2O buffer content. Differences in the apparent T-1 times allowed us to derive exchange rates for multiple residues in the type III secretion system needle protein.