Informace o publikaci

Understanding the methyl-TROSY effect over a wide range of magnetic fields

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BOLIK-COULON N. COUSIN A.F. KADEŘÁVEK Pavel DUMEZ J.N. FERRAGE F.

Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Chemical Physics
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
WWW https://aip.scitation.org/doi/10.1063/1.5095757
Doi http://dx.doi.org/10.1063/1.5095757
Klíčová slova MOLECULAR-WEIGHT PROTEINS; SIDE-CHAIN DYNAMICS; MODEL-FREE APPROACH; NMR-SPECTROSCOPY; RELAXATION; C-13; MACROMOLECULES; STRATEGIES; MOTIONS
Popis The use of relaxation interference in the methyl Transverse Relaxation-Optimized SpectroscopY (TROSY) experiment has opened new avenues for the study of large proteins and protein assemblies in nuclear magnetic resonance. So far, the theoretical description of the methyl-TROSY experiment has been limited to the slow-tumbling approximation, which is correct for large proteins on high-field spectrometers. In a recent paper, favorable relaxation interference was observed in the methyl groups of a small protein at a magnetic field as low as 0.33 T, well outside the slow-tumbling regime. Here, we present a model to describe relaxation interference in methyl groups over a broad range of magnetic fields, not limited to the slow-tumbling regime. We predict that the type of multiple-quantum transition that shows favorable relaxation properties change with the magnetic field. Under the condition of fast methyl-group rotation, methyl-TROSY experiments can be recorded over the entire range of magnetic fields from a fraction of 1 T up to 100 T.