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Postdoctoral Fellow

Shamayeeta Ray

Postdoctoral Fellow

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I trained as a chemist during my undergraduate. Considering my long-term interest in understanding the molecular and cellular basis of various biological processes, I shifted to Biotechnology in my Masters’ program. During this time I trained in a molecular biophysics lab where I got substantial exposure in protein biochemistry. This fruitful experience drove me to pursue my PhD in structural biochemistry where I enriched my knowledge and expertise further in understanding the molecular level pictures of how proteins function, using X-ray crystallography as the primary tool. My research focused on X-ray structure determination of a AAA+ regulator, MopR, belonging to the NtrC subfamily that is involved in direct sensing of toxic aromatic pollutants like phenol and their derivatives from the environment and directing them to their respective catabolic pathways for degradation. Based on the structural knowledge of ligand binding and substrate specificity, I successfully designed a spectrum of highly sensitive and selective targeted protein-based biosensors with real-time potential for direct detection of phenols and benzenes. My other work involved X-ray structural characterization of a TetR family regulator, TylP, from Streptomyces fradiae, which controls the levels of the commercially important antibiotic tylosin within the cell. I gained extensive knowledge and expertise in the field of molecular biology, X-ray crystallography, molecular biophysics and biochemistry, including isothermal titration calorimetry, circular dichroism, thermal melt assay, fluorescence spectroscopy, surface plasmon resonance etc. I also worked in close collaboration with a synchrotron scientist, Dr. Santosh Panjikar (my co-supervisor during PhD) in the Australian Synchrotron for 6 months, which has provided me with immense technical exposure in the protein crystallography field.

In my postdoctoral research, I am extending to transport proteins including membrane-bound channels and secondary transporters. In one project, I focus on work related to this AHA grant, to understand the molecular mechanisms of ligand binding and substrate selectivity for a transient receptor potential (TRP) ion channel, TRPA1. Using my expertise on ligand binding and specificity analysis, I investigate TRPA1 mutants and explore their ligand-binding affinity, selectivity, and channel activity using biochemical and functional assays. I will also advise and train other lab members also working on this project. In a second project, I focus on structural and biochemical characterization of substrate selectivity and conformational changes in NRAMPs (natural resistance-associated macrophage proteins), a conserved class of transition metal transporters that maintain the physiological levels of essential divalent metal ions. Both projects have analogous goals and thus synergize allowing me to reapply my skills to similar problems on two important protein families. I am confident that I can successfully contribute to this AHA project on TRPA1, applying my deep knowledge of protein biochemistry and ligand-binding specificity.