Research

Dr. Benedetta Sampoli Benitez


Ongoing Research

During the Summer of 2002, as a NYU Scholar In Residence, Dr. Sampoli Benitez started a collaboration with Dr. Tamar Schlick in Computational Biology. The goal of this research is to model the interaction of DNA polymerase X (PolX) with its target DNA. PolX is a protein involved in the DNA repair mechanism that is found in the African swine fever virus. It is the smallest known nucleotide transferase and is the least faithful, or more error prone, of all DNA polimerases studied so far. It has been suggested that this low fidelity might play a role in the virus mutagenesis. Since polX shares structural and functional similarities with human DNA polymerase beta,(pol b), a very well studied polymerase, in collaboration with Dr. L. Yang, Dr. Sampoli Benitez is planning to investigate polX fidelity mechanism by performing dynamics simulations for PolX/DNA complexes and comparing them with those of pol b (Yang et al. 2001, 2002).

Previous Research

At UCSD for her doctoral dissertation, Dr. Sampoli Benitez worked on the structure and dynamics of EGF-like domains of thrombomodulin (TM), a cell-surface glycoprotein that plays a regulatory role in the blood coagulation cascade. After solving the NMR solution structure of TM fragments necessary for thrombin binding (Sampoli Benitez et al. 1997, Wood et al. 2000 ), she performed 15N relaxation studies to investigate the dynamics of TM. She also utilized other biophysical methods, like analytical ultracentrifugation and fluorescence anisotropy, to determine the hydrodynamics properties of TM and its overall tumbling rate.

During her postdoctoral work at Memorial Sloan Kettering Cancer Center, Dr. Sampoli Benitez investigated the proteins involved in the actin cytoskeleton signal transduction pathway.