I am a physical biochemist with a deep curiosity about proteins, our molecular machines: what they look like, and how their structure informs their function. Particularly, I am interested in studying how small molecules and ligands are ferried across our cell membrane with the aid of proteins known as transporters — a type of phenomena which mediates many critical biological processes in a living organism.  This field of research lies at the intersection of chemistry, biology and physics, with immense scope for interdisciplinary research. Prior to Reed, I obtained my PhD in Physics from Stony Brook University in 2009. I was first introduced to biophysics in Dr. Steven O. Smith’s lab where, for my doctoral thesis, I used nuclear magnetic resonance (NMR) spectroscopy to study how the protein in our eyes, rhodopsin, respond to light photons and kick-start the signaling pathway to the brain that allows us to “see” in the dark. I was amazed by how I could use strong magnetic fields and radiofrequency pulses to manipulate magnetically active nuclei of hydrogen (¹H), carbon (¹³C) and nitrogen (¹⁵N) in rhodopsin to probe their chemical environment and study structural changes induced within when the protein absorbs the energy from a photon of light. 

I further built upon this interdisciplinary foundation by studying challenging biomolecular systems during my postdoctoral stints at both University of Michigan and Oregon Health & Science University in Portland. I have also spent time as a postdoctoral research fellow at Genentech, Inc. where I studied a human voltage-gated sodium channel protein, Nav1.7, which is central to our perception of pain. Throughout this journey, my primary focus has been on deciphering intricate and vital biomolecular protein systems using a range of biochemical assays and diverse biophysical methodologies such as NMR spectroscopy, X-ray crystallography, fluorescence spectroscopy and more recently cryogenic electron microscopy (Cryo-EM), and mass photometry.

Currently at Reed, my students and I are interested in understanding how bacteria maintains that delicate balance of metal ions such as manganese (Mn) and zinc (Zn) essential for its survival and pathogenicity. We are focused on structurally and functionally characterizing the different bacterial proteins that regulate the acquisition and efflux of these metal ions from the environment. Our research is looking at these protein systems in a model gram-positive bacterium, Bacillus subtilis, with the intention of expanding the knowledge gained to pathogenic bacteria. At Reed I teach a general chemistry course (Chem102) as well as structural biochemistry (Chem391) and a physical chemistry lecture & laboratory (Chem315) course. In my time away from the classroom and labs, I enjoy doing puzzles, Legos, crafting, cooking, camping, and going for long bike rides with my husband, and our ten-year-old daughter.

ABC’s of Metal ion Homeostasis: Importance for Bacterial Survival and Virulence

Pathogenic multidrug resistant bacterial infections are a leading cause of life-threatening human diseases such as pneumonia, tuberculosis, and osteomyelitis. During a bacterial infection, the host employs antimicrobial strategies against the pathogen including bombarding the bacteria with reactive oxygen species (ROS) and sequestration of essential nutrients like metal ions (manganese (Mn) and zinc (Zn)). Strains of bacteria have proven remarkably successful at overcoming these and other innate immune strategies employed by the host. Pathogenic bacteria have evolved robust virulence factors including the action of Mn and Zn ATP-Binding Cassette (ABC) importers, their corresponding efflux transporters and the transcription regulators that work together to successfully confront host sequestration strategies. Despite their importance, the structural basis for their function is poorly understood. Hence, my students and I are using a combination of single-particle cryogenic-electron microscopy (cryo-EM), fluorescence spectroscopy, and a variety of biochemical assays to structurally and functionally characterize the synergistic interplay between these different bacterial proteins in the regulation of nutrient acquisition, survival and virulence of pathogenic bacteria. Our research is looking at these protein systems in a model gram-positive bacterium, Bacillus subtilis, with the intention of expanding the knowledge gained to pathogenic bacteria. The mechanistic insights garnered from such a structurally driven study will not only shed light on the workings of the larger family of such transporters and transcription regulators but will also open new avenues for the development of innovative therapeutics to inhibit these deadly pathogens.