Automated test apparatus for bench-testing the magnetic field homogeneity of NMR transceiver coils.

We describe an automated hands-off bench testing method for measuring the magnetic field profile of transceiver coils for nuclear magnetic resonance (NMR). The scattering parameter (S-parameter) data is measured using a portable network analyzer, and the results are automatically exported to a computer for plotting and viewing. This assay dramatically reduces the time needed to measure the magnetic field (B) homogeneity profile of a transceiver coil while also improving accuracy relative to manual operation.

Reimagining magnetic resonance instrumentation using open maker tools and hardware as protocol.

Over the course of its history, the field of nuclear magnetic resonance spectroscopy has been characterized by alternating periods of intensive instrumentation development and rapid expansion into new chemical application areas. NMR is now both a mainstay of routine analysis for laboratories at all levels of education and research. On the other hand, new instrumentation and methodological advances promise expanded functionality in the future.

3D-printed dissolvable inserts for efficient and customizable fabrication of NMR transceiver coils.

We describe a simplified method for improving the reproducibility of transceiver coil fabrication for nuclear magnetic resonance (NMR) through single-use templates made from 3D-printed polymer forms. The utility of dissolvable inserts for achieving performance enhanced resonators (DIAPERs) is tested herein by a comparison of RF homogeneity along the rotor axis for variable-pitch solenoids with different inter-turn spacing. Simulated B field profiles are compared to experimental homogeneity measurements, demonstrating the potential of this approach for making NMR coils quickly and reproducibly.

Advances in instrumentation and methodology for solid-state NMR of biological assemblies.

Many advances in instrumentation and methodology have furthered the use of solid-state NMR as a technique for determining the structures and studying the dynamics of molecules involved in complex biological assemblies. Solid-state NMR does not require large crystals, has no inherent size limit, and with appropriate isotopic labeling schemes, supports solving one component of a complex assembly at a time. It is complementary to cryo-EM, in that it provides local, atomic-level detail that can be modeled into larger-scale structures.

Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules.

Extensive deuteration is frequently used in solid-state NMR studies of biomolecules because it dramatically reduces both homonuclear (H-H) and heteronuclear (H-C and H-N) dipolar interactions. This approach greatly improves resolution, enables low-power rf decoupling, and facilitates H-detected experiments even in rigid solids at moderate MAS rates. However, the resolution enhancement is obtained at some cost due the reduced abundance of protons available for polarization transfer.