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Old 09-30-2011, 08:01 PM
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Default Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange

Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange


Abstract Although originally designed for broadband inversion and decoupling in NMR spectroscopy, recent methodological developments have introduced adiabatic fast passage (AFP) pulses into the field of protein dynamics. AFP pulses employ a frequency sweep, and have not only superior inversion properties with respect to offset effects, but they are also easily implemented into a pulse sequence. As magnetization is dragged from the +z to the â??z direction, Larmor precession is impeded since magnetization becomes spin-locked, which is a potentially useful feature for the investigation of microsecond to millisecond dynamics. A major drawback of these pulses as theoretical prediction is concerned, however, results from their time-dependent offset: simulations of spin density matrices under the influence of a time-dependent Hamiltonian with non-commuting elements are costly in terms of computational time, rendering data analysis impracticable. In this paper we suggest several ways to reduce the computational time without compromising accuracy with respect to effects such as cross-correlated relaxation and modulation of the chemical shift.

  • Content Type Journal Article
  • Category Article
  • Pages 35-47
  • DOI 10.1007/s10858-011-9539-8
  • Authors
    • Renate Auer, Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria
    • Martin Tollinger, Department of Organic Chemistry, Leopold Franzens Universitaet Innsbruck, Innrain 52a, 6020 Innsbruck, Austria
    • Ilya Kuprov, Oxford e-Research Centre, University of Oxford, 7 Keble Road, Oxford, OX1 3QG UK
    • Robert Konrat, Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria
    • Karin Kloiber, Department of Organic Chemistry, Leopold Franzens Universitaet Innsbruck, Innrain 52a, 6020 Innsbruck, Austria


Source: Journal of Biomolecular NMR
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