Lois Pollack

Lois Pollack


  • Advisor
  • Molecular Architecture of Life


  • Cornell University
School of Applied and Engineering Physics


  • United States


BA, Brandeis University
PhD, Massachusetts Institute of Technology


Lois Pollack’s training is in experimental condensed matter physics, a field that she pursued through graduate school and postdoctoral study.

In 1996 she read a paper about protein folding, which dramatically changed her perspective on science. She retrained in biophysics and, in collaboration with several mentors, demonstrated a new technology to monitor the earliest events in protein folding. As a faculty member in Cornell’s School of Applied and Engineering Physics, her primary research interest is in developing and applying methods that provide previously inaccessible information about the dynamics of biological macromolecules. Much of her work focuses on the nucleic acids. These macromolecules are biologically essential, and serve as both drug targets and therapeutic agents. Our detailed understanding of DNA and RNA is in early stages, largely because of the substantial negative charge of the nucleic acid backbone, as well as the high flexibility of non-based paired RNA. Pollack’s work often highlights the partners that enable RNA folding and function. She is also interested in applying state of the art experimental tools, such as X-ray Free Electron Lasers, to study the dynamics of biomolecules. Currently, her lab develops technologies that uniquely enable investigations of the molecular mechanisms behind antibiotic resistance.

Relevant Publications

Plumridge, A., A. Katz, G. Calvey, R. Elber, S. Kirmizialtin and L. Pollack. “Revealing the distinct folding phases of an RNA three-helix junction.” Nucleic Acids Res., 46, 7354-7365 (2018).

Olmos, J.L. Jr. et al., "Enzyme intermediates captured "on-the-fly" by mix-and-inject serial crystallography." BMC Biology, 16, 59 (2018).

Chen, Y., J.M. Tokuda, T. Topping, S.P. Meisburger, S.A. Pabit, L.M. Gloss and L. Pollack. “Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the histone core.” Proc. Natl. Acad. Sci USA, 114, 2 (2017): 334-339.

H. Chen*, S. P. Meisburger*, S.A. Pabit, J. L. Sutton, W.W. Webb and L. Pollack. “ The ionic strength dependent persistence length of single stranded RNA and DNA”, Proc. Natl Acad Sci USA, 109, 3 (2012): 799-804.

Pollack, L. “SAXS studies of ion-nucleic acid interactions.” Annu. Rev. Biophys., 40 (2011): 225–42.