2019/03/31 by Nicolas Bolik-Coulon, Samuel F. Cousin, Pavel Kadeřávek +2 · 7 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Advanced NMR Techniques and Applications #Interference (communication) #Magnetic field #Magnetic relaxation #NMR spectroscopy and applications #Protein Structure and Dynamics #Range (aeronautics) #Relaxation (psychology) #Spectroscopy #physics.chem-ph
paper · pdf · doi:10.1063/1.5095757
published in The Journal of Chemical Physics 150(22), 224202 (American Institute of Physics)
openalex created_date 2019/03/22 · arxiv created 2019/05/07 · openalex publication_date 2019/06/14 · arxiv updated 2019/07/24 · openalex updated_date 2026/08/05
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.