Publication details
Understanding the methyl-TROSY effect over a wide range of magnetic fields
| Authors | |
|---|---|
| Year of publication | 2019 |
| Type | Article in Periodical |
| Magazine / Source | Journal of Chemical Physics |
| MU Faculty or unit | |
| Citation | |
| Web | https://aip.scitation.org/doi/10.1063/1.5095757 |
| Doi | http://dx.doi.org/10.1063/1.5095757 |
| Keywords | MOLECULAR-WEIGHT PROTEINS; SIDE-CHAIN DYNAMICS; MODEL-FREE APPROACH; NMR-SPECTROSCOPY; RELAXATION; C-13; MACROMOLECULES; STRATEGIES; MOTIONS |
| Description | 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. |