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Journal Article

Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR.

MPS-Authors
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Giller,  K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Supplementary Material (public)

2492804_Suppl.docx
(Supplementary material), 28KB

Citation

Chevelkov, V., Giller, K., Becker, S., & Lange, A. (2017). Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR. Journal of Magnetic Resonace, 283, 110-116. doi:10.1016/j.jmr.2017.08.012.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-19FF-F
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.