Ultrahigh-resolution solid-state NMR for high-molecular weight proteins on GHz-class spectrometers.

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique with broad impact across the physical and life sciences, and ultrahigh field (UHF), gigahertz-class NMR spectrometers offer exceptional performance, including superior resolution and sensitivity. In solid-state NMR (SSNMR), resolution is primarily constrained by instrumentation rather than molecular tumbling, making it well suited for studying large and complex systems. To fully leverage UHF magnets for SSNMR, it is essential to eliminate line broadening arising from magnetic field drift and couplings among the nuclear spins.

Ultra-High Resolution Solid-State NMR for High Molecular Weight Proteins on GHz-Class Spectrometers.

Unlabelled: NMR spectroscopy is a powerful technique with broad impact across the physical and life sciences, and ultra-high field, GHz-class NMR spectrometers offer exceptional overall performance including superior resolution and sensitivity. While the resolution is fundamentally limited by molecular tumbling for solution NMR, solid-state NMR (SSNMR) is constrained only by instrumentation, making it well-suited for studying large and complex systems. To fully leverage UHF magnets for magic-angle-spinning SSNMR, it is essential to eliminate linebroadening arising from magnetic field drift and couplings among the nuclear spins.

Probe design for high sensitivity proton-detected solid-state NMR.

Proton (H) detection methodologies in solid-state NMR (SSNMR) have revolutionized the field allowing for probing of new frontiers in determining the structure and dynamics within biological systems and materials. While approaches that maximally leverage the high gyromagnetic ratio of H detection have enhanced sensitivity and resolution of SSNMR experiments, the radiofrequency (rf) circuit of magic-angle spinning (MAS) probes is not well optimized for H detection, limiting the overall signal-to-noise ratio (SNR). Rather, SSNMR probes have historically been optimized for lower gamma nuclei such as C and below.

Magnetic Susceptibility Modeling of Magic-Angle Spinning Modules for Part Per Billion Scale Field Homogeneity.

Magic-angle spinning (MAS) solid-state NMR methods are crucial in many areas of biology and materials science. Conventional probe designs have often been specified with 0.1 part per million (ppm) or 100 part per billion (ppb) magnetic field resolution, which is a limitation for many modern scientific applications.

Indirectly detected heteronuclear correlation solid-state NMR spectroscopy of naturally abundant 15N nuclei.

Two-dimensional indirectly detected through-space and through-bond (1)H{(15)N} solid-state NMR experiments utilizing fast magic angle spinning (MAS) and homonuclear multipulse (1)H decoupling are evaluated. Remarkable efficiency of polarization transfer can be achieved at a MAS rate of 40 kHz by both cross-polarization and INEPT, which makes these methods applicable for routine characterizations of natural abundance solids. The first measurement of 2D (1)H{(15)N} HETCOR spectrum of natural abundance surface species is also reported.

Reduction of RF-induced sample heating with a scroll coil resonator structure for solid-state NMR probes.

Heating due to high power 1H decoupling limits the experimental lifetime of protein samples for solid-state NMR (SSNMR). Sample deterioration can be minimized by lowering the experimental salt concentration, temperature or decoupling fields; however, these approaches may compromise biological relevance and/or spectroscopic resolution and sensitivity. The desire to apply sophisticated multiple pulse experiments to proteins therefore motivates the development of probes that utilize the RF power more efficiently to generate a high ratio of magnetic to electric field in the sample.