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Heteronuclear relaxation in time-dependent spin systems: 15N-T1ρ dispersion during adiabatic fast passage

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Abstract

A novel NMR experiment comprising adiabatic fast passage techniques for the measurement of heteronuclear self-relaxation rates in fully 15N-enriched proteins is described. Heteronuclear self-relaxation is monitored by performing adiabatic fast passage (AFP) experiments at variable adiabaticity (e.g., variation of RF spin-lock field intensity). The experiment encompasses gradient- selection and sensitivity-enhancement. It is shown that transverse relaxation rates derived with this method are in good agreement with the ones measured by the classical Carr–Purcell–Meiboom–Gill (CPMG) sequences. An application of this method to the study of the carboxyl-terminal LIM domain of quail cysteine and glycine-rich protein qCRP2(LIM2) is presented.

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Authors and Affiliations

  1. Institute of Organic Chemistry, University of Innsbruck, A- 6020, Innsbruck, Austria

    Robert Konrat & Martin Tollinger

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  1. Robert Konrat
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  2. Martin Tollinger
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Konrat, R., Tollinger, M. Heteronuclear relaxation in time-dependent spin systems: 15N-T1ρ dispersion during adiabatic fast passage. J Biomol NMR 13, 213–221 (1999). https://doi.org/10.1023/A:1008324721356

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