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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 |

REPOSITORIES: biostudies-literature

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