We show the design, simulations, and experimental performance of a 35 GHz electron paramagnetic resonance (EPR) resonator based on a cylindrical cavity with 3 mm sample access. The design is robust; simple to manufacture and maintain; and, with its elevated Q value, well-suited to sensitive EPR experiments using continuous-wave or low-power pulsed excitation. Thus, we make multi-frequency EPR spectroscopy, a powerful approach to deconvolute overlapping paramagnetic species, more accessible.

We introduce the PRESERVE pulse sequence element, allowing variable flip-angle adjustment in 2D ¹H–¹⁵N and ¹H–¹³C transverse-relaxation-optimized-spectroscopy (TROSY)-type correlation experiments. PRESERVE-TROSY exploits a remarkable array of up to nine orthogonal polarization-coherence transfer pathways, showcasing the remarkable potential of spin manipulations achievable via the design and optimization of nuclear magnetic resonance (NMR) pulse sequences.

The nuclear magnetic resonance (NMR) spectroscopy of the ¹⁰³Rh nucleus is onerous owing to its dismal sensitivity. Here, we utilise modern techniques to boost the sensitivity and acquire valuable ¹⁰³Rh NMR parameters for the Rh(acac)₃ transition-metal complex. We acquire proton-enhanced ¹⁰³Rh NMR spectra and successfully characterise the ¹⁰³Rh spin relaxation. In doing so, we unveil the secrets of a complex that is of significant interest to the ¹⁰³Rh NMR and wider chemical community alike.

Scalar couplings give rise to peak splitting in nuclear magnetic resonance (NMR) spectra. Couplings between atoms that span a rotatable bond report on the rotation angle of the bond. Here, we describe a new computational method that can be used to analyze complex patterns of peak splitting. In addition to showing new ways of visualizing and analyzing the underlying data, we uncover how isolated parts of proteins behave differently than when they are embedded in a folded protein.