title: 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.
authors.affiliation: Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland.
authors.forename: Thomas
authors.initials: T
authors.lastname: Westfeld
authors.forename: René
authors.initials: R
authors.lastname: Verel
authors.forename: Matthias
authors.initials: M
authors.lastname: Ernst
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
mesh_terms: D003198:Computer Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins