Properties of the DREAM scheme and its optimization for application to proteins.

Journal of Biomolecular NMR
Thomas WestfeldB H Meier

Abstract

The DREAM scheme is an efficient adiabatic homonuclear polarization-transfer method suitable for multi-dimensional experiments in biomolecular solid-state NMR. The bandwidth and dynamics of the polarization transfer in the DREAM experiment depend on a number of experimental and spin-system parameters. In order to obtain optimal results, the dependence of the cross-peak intensity on these parameters needs to be understood and carefully controlled. We introduce a simplified model to semi-quantitatively describe the polarization-transfer patterns for the relevant spin systems. Numerical simulations for all natural amino acids (except tryptophane) show the dependence of the cross-peak intensities as a function of the radio-frequency-carrier position. This dependency can be used as a guide to select the desired conditions in protein spectroscopy. Practical guidelines are given on how to set up a DREAM experiment for optimized Cα/Cβ transfer, which is important in sequential assignment experiments.

References

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Citations

Nov 19, 2013·Journal of Biomolecular NMR·Lucio FerellaAntonio Rosato
Mar 24, 2015·Journal of Magnetic Resonance·Anja BöckmannBeat H Meier
Aug 19, 2015·The Journal of Physical Chemistry Letters·Kong Ooi TanMatthias Ernst
Feb 6, 2017·Journal of Biomolecular NMR·Thomas BauerBeat H Meier
Nov 30, 2019·Progress in Nuclear Magnetic Resonance Spectroscopy·Amir Goldbourt
Dec 14, 2017·Solid State Nuclear Magnetic Resonance·Kong Ooi TanMatthias Ernst
Jun 15, 2017·Journal of the American Chemical Society·Daryl GoodVladimir Ladizhansky

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