Solid-State NMR Spectroscopy Techniques and Applications

Solid-state nuclear magnetic resonance (NMR) spectroscopy has evolved into a versatile tool for elucidating structural and dynamic features of materials, biomolecules and complex assemblies that are inaccessible by conventional solution-state methods. By employing high magnetic fields and advanced pulse sequences, solid-state NMR offers atomic-level insights into crystalline and amorphous systems alike, ranging from pharmaceutical formulations and battery electrode materials to membrane proteins and nucleic acids. Key technical advances—such as magic-angle spinning (MAS), dynamic nuclear polarisation (DNP) and refined recoupling schemes—have dramatically improved sensitivity and resolution. These innovations enable the measurement of chemical shift anisotropies, dipolar couplings and relaxation rates, thereby permitting quantification of local order parameters and motional time scales spanning picoseconds to milliseconds. Applications span the determination of metal speciation in functional materials, the characterisation of conformational exchange in protein crystals and the de novo structure determination of RNA elements within large ribonucleoprotein complexes. Together, these developments underscore the global significance of solid-state NMR as a non-invasive probe of structure, dynamics and interactions in diverse scientific and industrial contexts.

Research from Nature Portfolio

Recent studies have harnessed dynamic nuclear polarisation to overcome inherent sensitivity limits in solid-state NMR, enabling the direct observation of low-abundance nuclei in complex matrices. One investigation demonstrated that DNP-enhanced 119Sn experiments can discriminate Sn(II) and Sn(IV) species in commercial toothpaste, resolving oxidation states and quantifying their populations. Complementary work on protein crystals employed near-rotary-resonance relaxation dispersion to reveal microsecond-scale conformational exchange in ubiquitin, showing how crystal packing modulates both local backbone motions and overall rocking of protein molecules. Another foundational study extended solid-state NMR to RNA by combining segmental labelling with tailored recoupling schemes, achieving high-resolution structures of RNA fragments within megadalton ribonucleoprotein assemblies. Together, these contributions illustrate how sensitivity enhancements and bespoke pulse programmes are unlocking new frontiers in materials chemistry, structural biology and nucleic acid research.

Research from all publishers

Advances outside the portfolio have further refined the toolkit of solid-state NMR. Recent work on relaxation dispersion under MAS demonstrated that R1ρ experiments can characterise microsecond-to-millisecond dynamics in large enzymes and membrane proteins, exploiting both chemical-shift fluctuations and dipolar interactions. Another study revealed that ultrafast MAS rates up to 160 kHz, in conjunction with a 1.2 GHz proton Larmor frequency, markedly enhance spectral resolution of protein side-chain 1H resonances, facilitating comprehensive proton assignments in viral capsids. In the realm of paramagnetic systems, a thorough theoretical and practical treatment unified descriptions of paramagnetic shifts and relaxation in solids, integrating magnetic susceptibility and spin-orbit coupling effects to enable accurate interpretation of spectra from lanthanide-doped materials, metalloproteins and battery electrodes. Collectively, these developments have expanded the observable parameter space and improved quantitative analyses of complex systems.

Solid-State NMR Spectroscopy Techniques and Applications publication trend

The graph below shows the total number of articles in solid-state nmr spectroscopy techniques and applications across all publications each year (not limited to Nature Index journals).

Technical terms

Magic-Angle Spinning (MAS): Rapid rotation of the sample at 54.74° relative to the static magnetic field to average out anisotropic interactions and narrow spectral lines.

Dynamic Nuclear Polarisation (DNP): Transfer of polarisation from unpaired electrons to nuclear spins, boosting NMR signal intensities by several orders of magnitude.

Chemical Shift Anisotropy (CSA): Variation of the NMR chemical shift with molecular orientation in the magnetic field, providing information on electronic environments.

Relaxation Dispersion: Measurement of relaxation rates as a function of spin-lock or field-offset frequency to probe conformational exchange processes on microsecond to millisecond time scales.

References

1. Structural characterization of tin in toothpaste by dynamic nuclear polarization enhanced 119Sn solid-state NMR spectroscopy. Nature Communications (2023).
2. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications (2017).
3. RNA structure determination by solid-state NMR spectroscopy. Nature Communications (2015).
4. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology (2023).
5. High and fast: NMR protein–proton side-chain assignments at 160 kHz and 1.2 GHz. Chemical Science (2023).
6. Paramagnetic NMR in solution and the solid state. Progress in Nuclear Magnetic Resonance Spectroscopy (2018).