• Organization
    Cornell University

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    (607) 255-8695

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    Lois Pollack
    School of Applied and Engineering Physics
    Clark Hall 254
    Ithaca, NY 14853

  • Biography

    Lois Pollack’s research program has two distinct themes. The first theme is instrumentation: the development of experimental tools that enable novel, time-resolved studies of proteins, DNA or RNA. By coupling microfluidics with light (either X-rays or lasers). Her group has developed and applied tools that report dynamic shape changes as these large molecules assume (‘fold’ to) their biologically active states. The second theme is a tight research focus on electrostatic interactions in RNA and DNA. The large negative charge carried by these nucleic acids significantly impacts their structure and function. This topic is timely, as recognition of RNA’s central role in the cell continues to increase at an astonishing rate.

    Dr. Pollack received her Ph.D. in Condensed Matter Physics from the Massachusetts Institute of Technology, and then went to work at Cornell in the Low Temperature Physics group. She was a Postdoctoral Associate (1989-1991) and a Research Associate (1991-1997) in the Microkelvin Laboratory. In 1997, with support from the NSF and the LASSP Biophysics Group, she changed the focus of her research program to biophysics. In 1999, she became Senior Research Associate in LASSP. She joined the Cornell faculty in Applied and Engineering Physics, in 2000.

    As part of the BioXFEL Center, the Pollack Lab, which specializes in developing new instrumentation to advance small angle X-ray scattering studies of proteins, RNA and DNA will focus its efforts on time-resolved SAXS as a probe of conformational dynamics and folding. In the past, they applied microfluidic mixers to trigger and monitor protein and RNA folding using SAXS. The group has also developed a microfluidic cell to trigger and measure light-dependent protein conformational changes. X-ray free electron laser sources present new opportunities for determining solution structures of bio-molecules based on analyzing angular correlations within individual SAXS profiles. Their successful demonstration of these new methods will enable time-resolved studies of structural changes, initiated either by laser flash, or by rapid solvent exchange.

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