caa a22 4500 445325550 CHVBK 20180317142719.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s10858-011-9539-8 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9539-8 Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange [Elektronische Daten] [Renate Auer, Martin Tollinger, Ilya Kuprov, Robert Konrat, Karin Kloiber] 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 −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. The Author(s), 2011 NMR nationallicence Adiabatic fast passage nationallicence Microsecond-millisecond dynamics nationallicence Auer Renate Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut Tollinger Martin Department of Organic Chemistry, Leopold Franzens Universitaet Innsbruck, Innrain 52a, 6020, Innsbruck, Austria aut Kuprov Ilya Oxford e-Research Centre, University of Oxford, 7 Keble Road, OX1 3QG, Oxford, UK aut Konrat Robert Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut Kloiber Karin Department of Organic Chemistry, Leopold Franzens Universitaet Innsbruck, Innrain 52a, 6020, Innsbruck, Austria aut Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 35-47 0925-2738 51:1-2<35 2011 51 10858 https://doi.org/10.1007/s10858-011-9539-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9539-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Auer Renate Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut NATIONALLICENCE 700 1- Tollinger Martin Department of Organic Chemistry, Leopold Franzens Universitaet Innsbruck, Innrain 52a, 6020, Innsbruck, Austria aut NATIONALLICENCE 700 1- Kuprov Ilya Oxford e-Research Centre, University of Oxford, 7 Keble Road, OX1 3QG, Oxford, UK aut NATIONALLICENCE 700 1- Konrat Robert Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut NATIONALLICENCE 700 1- Kloiber Karin Department of Organic Chemistry, Leopold Franzens Universitaet Innsbruck, Innrain 52a, 6020, Innsbruck, Austria aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 35-47 0925-2738 51:1-2<35 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer