Rachel Leeman

 Rachel Leeman
Mentor: Dr. Ben Dunn
College of Medicine
"I initially got involved with research because I wanted to gain a unique perspective on science and problem solving outside of the classroom. It is one thing to learn about various processes and chemical equations from a professor or in a textbook, and another entirely to experience it all first hand. My involvement in research has kept learning exciting while also exposing me to many long-term skills beneficial to my future."





Research Interests

  • Biochemistry/Molecular Biology
  • Drug Target Discovery
  • Infectious Diseases

Academic Awards

  • UF University Scholars Program
  • Dean's List


  • Alpha Epsilon Phi
  • Just Shoe It
  • Dance Marathon


  • Footprints Buddy and Support Program at Shands Hospital
  • UF Hillel Alternative Spring Break
  • Boca Regional Hospital

Hobbies and Interests

  • Waterskiing
  • Swimming
  • Flag Football
  • Traveling

Research Description

Purification and Crystallization of XMRV Protease
Xenotropic murine leukemia virus-related virus is a retrovirus recently discovered in 2006 that has been linked to the development of prostate cancer. My project focuses on the expression, purification, and crystallization of XMRV protease complexed with strong inhibitors in order to identify a drug target for the protease. After the XMRV protease is expressed in a strain of E.coli, the protease must be purified. The protein is purified once using a nickel affinity chromatography column and then further purified using gel filtration chromatography. After enough purified protein is gathered, crystallographic trials will begin by complexing various aspartic protease inhibitors to the purified XMRV protease. The inhibition constants of each inhibitor were determined kinetically with spectrophotometric analysis. Results from the crystallographic analyses will not only be useful for the development of a drug for prostate cancer, but also for identifying a drug target for HIV-1 protease since the two proteases are structurally similar.