Shivani Ahuja is a physical biochemist with a deep curiosity about proteins, our molecular machines: what they look like, and how their structure informs their function. This field of research lies at the intersection of chemistry, biology and physics, with immense scope for interdisciplinary research. Prior to Reed, Shivani obtained her PhD in Physics from Stony Brook University in 2009. For her doctoral thesis, she 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. She further built upon this interdisciplinary foundation by studying challenging biomolecular systems during her postdoctoral stints at both University of Michigan and Oregon Health & Science University in Portland. She also spent time as a postdoctoral research fellow at Genentech, Inc. where she studied a human voltage-gated sodium channel protein, Nav1.7, which is central to our perception of pain. Throughout this journey, her 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, Shivani and her students are interested in understanding how bacteria maintains that delicate balance of metal ions such as manganese and zinc essential for its survival and pathogenicity. They are focused on structurally and functionally characterizing the different bacterial proteins that regulate the acquisition and efflux of these metal ions from the environment. Shivani's lab also collaborates with Dr. Jay Mellies' lab in the Biology Department to grow a microbial consortium on polyethylene terephthalate (PET) and polyethylene (PE) and analyze degradation products via NMR. This provides insights into (1) molecular structure and composition of degradation products and (2) PET and PE degradation kinetics, aiding in identifying enzymes involved. We are also structurally characterizing carboxylesterases identified by Mellies' lab for PET and mono-(2-hydroxyethyl) terephthalic acid (MHET) degradation.