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

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


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.

• Content Type Journal Article
• Category Article
• Pages 1-10
• DOI 10.1007/s10858-012-9627-4
• Authors
  • Thomas Westfeld, Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland
  • René Verel, Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland
  • Matthias Ernst, Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland
  • Anja Böckmann, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367 Lyon, France
  • Beat H. Meier, Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738

Source: Journal of Biomolecular NMR