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

2021 | journal article

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​Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning​
Nimerovsky, E.; Movellan, K. T.; Zhang, X. C.; Forster, M. C.; Najbauer, E.; Xue, K. & Dervişoǧlu, R. et al.​ (2021) 
Biomolecules11(5) pp. 752​.​ DOI: https://doi.org/10.3390/biom11050752 

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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.
Abstract
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.
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.
Issue Date
2021
Journal
Biomolecules 
eISSN
2218-273X
Language
English

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