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Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments.

MPG-Autoren
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Pratihar,  S.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Ban,  D.
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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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Zitation

Reddy, J. G., Pratihar, S., Ban, D., Frischkorn, S., Becker, S., & Griesinger, C. (2017). Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments. Journal of Biomolecular NMR, (in press). doi:10.1007/s10858-017-0155-0.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002E-8135-D
Zusammenfassung
Molecular dynamics play a significant role in how molecules perform their function. A critical method that provides information on dynamics, at the atomic level, is NMR-based relaxation dispersion (RD) experiments. RD experiments have been utilized for understanding multiple biological processes occurring at micro-to-millisecond time, such as enzyme catalysis, molecular recognition, ligand binding and protein folding. Here, we applied the recently developed high-power RD concept to the Carr–Purcell–Meiboom–Gill sequence (extreme CPMG; E-CPMG) for the simultaneous detection of fast and slow dynamics. Using a fast folding protein, gpW, we have shown that previously inaccessible kinetics can be accessed with the improved precision and efficiency of the measurement by using this experiment.