Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning

• Published in: Biomolecules (Basel, Switzerland) Switzerland), 2021-05, Vol.11 (5), p.752
• Main Authors: Nimerovsky, Evgeny, Movellan, Kumar Tekwani, Zhang, Xizhou Cecily, Forster, Marcel C, Najbauer, Eszter, Xue, Kai, Dervişoǧlu, Rıza, Giller, Karin, Griesinger, Christian, Becker, Stefan, Andreas, Loren B
• Format: Article
• Language: English
• Subjects: Bacterial Outer Membrane Proteins - chemistry; beta barrel; Geobacillus - metabolism; Humans; Influenza A virus - metabolism; Labeling; magic-angle spinning; Magnetic Fields; membrane protein; Membrane proteins; Membrane Proteins - chemistry; Metabolism; Models, Molecular; Neisseria gonorrhoeae - metabolism; Nitrogen; NMR; Nuclear magnetic resonance; Protein expression; Protein Kinases - chemistry; Protein Structure, Secondary; Proteins; proton detection; Proton Magnetic Resonance Spectroscopy - instrumentation; solid-state NMR; Spectrum analysis; transmembrane; Viral Matrix Proteins - chemistry; Voltage-Dependent Anion Channels - chemistry
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom11050752

The available magnetic field strength for high resolution NMR in persistent superconducting magnets has recently improved from 23.5 to 28 Tesla, increasing the proton resonance frequency from 1 to 1.2 GHz. For magic-angle spinning (MAS) NMR, this is expected to improve resolution, provided the sample preparation results in homogeneous broadening. We compare two-dimensional (2D) proton detected MAS NMR spectra of four membrane proteins at 950 and 1200 MHz. We find a consistent improvement in resolution that scales superlinearly with the increase in magnetic field for three of the four examples. In 3D and 4D spectra, which are now routinely acquired, this improvement indicates the ability to resolve at least 2 and 2.5 times as many signals, respectively.