Ilya Finkelstein, PhD

  • Recruited to: The University of Texas at Austin
  • Recruited from: Columbia University Medical Center
  • Award: First-Time, Tenure-Track Faculty Member

Dr. Ilya Finkelstein received his B.S. from the University of California at Berkeley and his Ph.D. in Chemistry from Stanford University with Professor Michael D. Fayer.  In 2007, he moved to the group of Prof. Eric C. Greene at Columbia University Medical Center as an NRSA Postdoctoral Fellow.  In 2012, Dr. Finkelstein joined the Department of Chemistry and Biochemistry and the Institute of Cellular and Molecular Biology at the University of Texas at Austin.  His current research is focused on understanding how our cells are able to stave off genomic instability and avoid cancer.

Dr. Finkelstein’s graduate research tackled the question of how a protein’s structural fluctuations are coupled to the solvation environment. Dr. Finkelstein discovered that proteins retain most of their mobility even when surrounded by as few as two aqueous solvation layers.  Indeed, protein dynamics persist even when a protein is encapsulated in a glassy matrix at room temperature

At Columbia University, Dr. Finkelstein’s research focused on addressing a fundamental and unresolved question in nucleic acid biochemistry:  How do DNA-binding motor proteins move on crowded DNA?  Inside living cells, molecular crowding may profoundly alter the behavior of DNA-binding motor proteins, which are involved in all aspects of DNA maintenance. Dr. Finkelstein directly visualized collisions between proteins as they travel along DNA and has contributed to our mechanistic understanding of this process.

At the University of Texas at Austin, Dr. Finkelstein’s lab focuses on understanding the molecular mechanisms of genome maintenance, including aspects of DNA repair, replication and chromatin biology.  He addresses these questions by combining biophysics, ultra-sensitive microscopy and micro-/nano-scale engineering to develop new tools for studying protein-DNA interactions at the single-molecule level.  He is continuing to advance the high-throughput “DNA curtains” microfluidics platform for imaging thousands of individual biochemical reactions in real-time.  Directly looking at proteins as they perform their biological functions allows his group to uncover mechanistic details that are obscured in traditional biochemical experiments.  Elucidating the mechanisms of DNA maintenance is critical to our understanding of both the molecular basis and the therapeutic treatment of devastating human diseases.