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.