Journal of Biomolecular NMR

, Volume 53, Issue 2, pp 103–112 | Cite as

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

  • Thomas Westfeld
  • René Verel
  • Matthias Ernst
  • Anja Böckmann
  • Beat H. Meier


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.


Solid-state NMR Recoupling DREAM 



Nuclear magnetic resonance


Magic-angle spinning




Dipolar recoupling enhanced by amplitude modulation


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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  1. 1.Physical ChemistryETH ZürichZurichSwitzerland
  2. 2.Institut de Biologie et Chimie des Protéines, UMR 5086 CNRSUniversité de Lyon 1LyonFrance

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