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Hobbies:
Biochemistry, Protein Crystallography, DNA metabolism, Breast Cancer, Physical Characterization of Protein Crystals and X-ray diffraction physics
My primary interest is in studying the macromolecules essential to the maintenance and replication of DNA. Survival and normal growth of cells rely on
the basic processes of DNA metabolism. The entire genome must be replicated reliably every cell cycle and any defect must be corrected. My laboratory
performs basic research on the protein-DNA and protein-protein interactions that govern DNA metabolic processes.
Radiation and chemical agents can damage cellular DNA and this damage can interfere with DNA replication and gene expression. DNA damage must
be repaired if the cell is to survive normally. Defects in DNA repair are linked to congenital malformations and increased susceptibility to cancer.
Eukaryotic cells use nucleotide excision repair and recombination-dependent repair to remove many types of damage from DNA.
My research is focused on studying the proteins involved in DNA metabolism using X-ray crystallography and molecular
modeling. We are determining the structure of human replication protein A (RPA) with X-ray crystallography. RPA is a single-stranded DNA binding protein that is a key player in
DNA metabolism. RPA was first discovered when it was recognized as being essential for DNA synthesis. Now we know that RPA is intrinsic to the
homologous recombination of DNA and to nucleotide excision DNA repair. Interactions between RPA and many proteins are critical for DNA
metabolism. For example, a protein-protein complex formed by RPA and repair factor XPA recognize damaged DNA in the first step of nucleotide
excision repair. Also, interactions between RPA and repair factor RAD52 are essential to homologous recombination. We are studying the structure of
RPA and RAD52 as well as RPA-RAD52 interactions by X-ray crystallography and computer
modeling.
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