Rachel W. Martin was born in Mesa, Arizona and grew up surrounded by the plants and animals of the Sonoran Desert. Her first undergraduate research project involved collecting NMR spectra of a peptide from rattlesnake venom. She earned her BS in Chemistry from Arizona State University in 1997. She then joined Kurt Zilm’s lab at Yale for graduate school, arriving shortly before the installation of (at the time) the world’s largest NMR magnet. The arrival of the big magnet, operating at 800 MHz ¹H Larmor frequency, was a thrilling event marred only by the lack of magic angle spinning (MAS) probes operating at that frequency. Dreams of high-resolution protein structures were delayed for two and a half years while she and Eric Paulson built a new balanced triple resonance MAS probe for protein experiments. She then developed a method for rapid batch crystallization of proteins, enabling fast, reproducible sample preparation for biological MAS. Some of the first high-resolution protein spectra were collected using this instrumentation and methodology. After finishing her PhD in 2002, she then moved on to postdoctoral research with Alex Pines at UC Berkeley, where she worked on a variety of problems related to performing NMR and MRI experiments under challenging experimental conditions. She and her lab mates built inhomogenous magnets, one-sided magnets, and spinning magnets for ex situ NMR, enabling novel experimental modalities outside the typical narrow-bore superconducting magnets. During this period, Martin developed her interest in NMR of oriented samples and biological semi-solids.

As a faculty member at UC Irvine, Martin has continued to develop unique NMR instrumentation. Her group has built contactless switched-angle spinning (SAS) probes for high-resolution NMR of liquid crystals and oriented biological membranes. They have developed stabilized bicelle mixtures that hold up well under the mechanical challenges of SAS, and also have a favorable useful temperature range for solution-state NMR. The Martin group has also built a quadruple-resonance MAS probe for ¹H/¹³C/²H/¹⁵N experiments, enabling the ²H that is often used to simplify the 1H spectra  of proteins to also provide information about structure and dynamics. Along the way, they have developed new transceiver coil designs for specific biological experiments. One recent line of work focuses on developing strategies for enabling more researchers to participate in fabricating NMR instrumentation using 3D printing and automation. Dissolvable coil templates, 3D printed mechanical components, and inexpensive automated test devices can make NMR instrumentation development more accessible. The goal is to ensure that the next generation can build and use custom instrumentation, which is historically one of the greatest strengths of the NMR community. On the applications side, the Martin group has explored the relationship between structure and optical properties in eye lens proteins, as well as discovering and characterizing novel proteins, notably a membrane-binding antimicrobial peptide. Since its founding in 2005, the Martin group has trained 7 postdoctoral fellows and 21 PhDs in a wide range of fields, including Physical Chemistry, Analytical Chemistry, Chemical Biology, Molecular Biology and Biochemistry, and Physics.