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Vassiliy Lubchenko


Vassiliy Lubchenko
Associate Professor
Ph.D., University of Illinois at Urbana-Champaign, 2002
M.S., Carnegie Mellon University, 1995
M.S., Moscow Institute of Physics and Technology, 1994

Department of Chemistry
University of Houston
Houston, Texas 77204-5003

Office: 212D - Fleming
Phone: 832.842.8853
Prof. Lubchenko's Benefunder profile
My research interests include strongly disordered and non-equilibrium systems, with specific applications to materials science, molecular electronics, and biophysics.

Our main focus is a self-consistent theory of structural and electronic excitations in amorphous materials. Several optical and electronic anomalies that are unique to semiconductor glasses have resisted systematic efforts for decades, including light induced ESR, midgap absorption, and insensitivity to conventional doping. Our findings show these anomalies are not a generic consequence of disorder, but, instead, result from the high structural degeneracy of glasses. An important component of our research is the prediction of the structure and glassforming ability of specific substances of interest in applications, a task currently inaccessible to computer technology.

As part of the materials science project, we are developing first principles descriptions of inelastic deformation and fracture failure of glasses, amorphous solids in general, and other complex materials. Recent, critical developments in microscopic theories of glass formation are being used to describe visco-elastic properties of disordered media. Stress, corrosion, and radiation induced cracking are of basic and practical interest.

As part of our biophysical research agenda, we are investigating the microscopics underlying recently discovered puzzling behaviors of concentrated protein solutions, in collaboration with Peter Vekilov's group. In conflict with traditional nucleation theories, long-living aggregates of mesoscopic size are found in such solutions. In addition to the basic significance of this problem, it is also important in the context of formation of various solid protein aggregates, such as crystals and protein fiber arrays implicated in sickle cell anemia.