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Optimized selection of slow-relaxing 13C transitions in methyl groups of proteins: application to relaxation dispersion.

ABSTRACT: Optimized selection of the slow-relaxing components of single-quantum 13C magnetization in 13CH3 methyl groups of proteins using acute (< 90°) angle 1H radio-frequency pulses, is described. The optimal selection scheme is more relaxation-tolerant and provides sensitivity gains in comparison to the experiment where the undesired (fast-relaxing) components of 13C magnetization are simply 'filtered-out' and only 90° 1H pulses are employed for magnetization transfer to and from 13C nuclei. When applied to methyl 13C single-quantum Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments for studies of chemical exchange, the selection of the slow-relaxing 13C transitions results in a significant decrease in intrinsic (exchange-free) transverse spin relaxation rates of all exchanging species. For exchanging systems involving high-molecular-weight species, the lower transverse relaxation rates translate into an increase in the information content of the resulting relaxation dispersion profiles.

SUBMITTER: Tugarinov V 

PROVIDER: S-EPMC7704780 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Optimized selection of slow-relaxing <sup>13</sup>C transitions in methyl groups of proteins: application to relaxation dispersion.

Tugarinov Vitali V   Karamanos Theodoros K TK   Clore G Marius GM  

Journal of biomolecular NMR 20201001 12

Optimized selection of the slow-relaxing components of single-quantum <sup>13</sup>C magnetization in <sup>13</sup>CH<sub>3</sub> methyl groups of proteins using acute (< 90°) angle <sup>1</sup>H radio-frequency pulses, is described. The optimal selection scheme is more relaxation-tolerant and provides sensitivity gains in comparison to the experiment where the undesired (fast-relaxing) components of <sup>13</sup>C magnetization are simply 'filtered-out' and only 90° <sup>1</sup>H pulses are emp  ...[more]

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