Thanks to a major technological breakthrough in solid-state nuclear magnetic resonance, scientists are pushing the boundaries of complex biomolecule analysis. The arrival of equipment capable of achieving record sample rotation speeds of 160 kilohertz paves the way for more detailed and sensitive characterisation of proteins, even in minute quantities. This innovation marks a turning point in structural biology.

Solid-state nuclear magnetic resonance (NMR) spectroscopy is a powerful tool for deciphering the properties of solids at the atomic scale. In recent years, it has found major applications in structural biology, making it possible to elucidate the three-dimensional architecture of crystalline proteins, enzymes aggregated in the form of amyloid fibrils, and membrane proteins inserted into their native lipid environment.

One of the key technical breakthroughs that made this possible is magic angle spinning, a method that involves rotating the sample at a precise angle relative to the magnetic field in order to reduce line widths and improve spectral resolution. Over the past two decades, the gradual miniaturisation of MAS rotors, and thus the increase in rotation speeds, has made it possible to exceed critical thresholds in sensitivity and resolution, transforming the ability of NMR to explore complex biological systems.

More information on the CNRS website

Reference

Pushing the Boundaries of Resolution in Solid-State Nuclear Magnetic Resonance of Biomolecules with 160 kHz Magic-Angle Spinning. Zhiyu Sun, Claire Ollier, Adrienn Rancz, Batiste Thienpont, Kristof Grohe, Lukas Becker, Armin Purea, Frank Engelke, Sebastian Wegner, James Sturgis, Tatyana Polenova, Tanguy Le Marchand & Guido Pintacuda. J. Am. Chem. Soc. 2025. DOI: https://doi.org/10.1021/jacs.5c02466