Rachel Martin is interested in the molecular factors determining protein stability, solubility, and aggregation.
Her lab develops and uses a variety of biophysical techniques, in particular nuclear magnetic resonance (NMR) instrumentation and experiments, for investigating the structures and dynamics of complex biomolecular systems.
One of her projects involves studying the crystallin proteins that provide the refractive power of the vertebrate eye lens. Unlike most proteins, which are continually degraded and recycled, these extraordinary proteins last a lifetime, remaining transparent at high concentrations. The Martin lab investigates the molecular structures of the individual proteins, the transparent hydrogel making up the lens, and the aggregates that form in cataract disease. They also investigate crystallin evolution, which requires comparative studies of lens proteins from other animals.
- Camille and Henry Dreyfus New Faculty Award, 2005
- Fellow of the American Association for the Advancement of Science, 2008
- NSF-CAREER, 2009
Bierma, Jan C., Kyle W. Roskamp, Aaron P. Ledray, Andor J. Kiss*, C.-H. Christina Cheng, and R.W. Martin*. “Controlling liquid-liquid phase separation in cold-adapted crystallin proteins from the Antarctic toothfish.” Journal of Molecular Biology 430 (24); (2018): 5151-5168.
Domarin Khago, Jan C. Bierma, Kyle W. Roskamp, Natalia Kozlyuk, and R.W. Martin*. “Protein refractive index increment is determined by conformation as well as compo- sition.” Journal of Physics: Condensed Matter 30 (43); (2018): 435101.
Collier, Kelsey A., Suvrajit Sengupta, Catalina A. Espinosa, John E. Kelly, Jessica I. Kelz, and R.W. Martin*. “Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules.” Journal of Magnetic Resonance 285 (2017): 8-17.
Unhelkar, Megha H., Vy T. Duong, Kaosoluchi N. Enendu, John E. Kelly, Seemal Tahir, Carter T. Butts*. and R.W. Martin*. “Structure prediction and network analysis of chitinases from the Cape sundew, Drosera capensis.” Biochimica et Biophysica Acta – General Subjects 1861 (3); (2017): 636-643 (2017).
Kingsley, Carolyn N., William D. Brubaker, Stefan Markovic, Anne Diehl, Amanda J. Brindley, Hartmut Oschkinat, and R.W. Martin*. “Preferential, specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.” Structure 12; (12)(2013): 2221-2227.
CIFAR is a registered charitable organization supported by the governments of Canada, Alberta and Quebec, as well as foundations, individuals, corporations and Canadian and international partner organizations.