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Biophysics Focus Area
Biophysics applies the principles of physics and chemistry and the methods of mathematical analysis and computer modeling to understand how biological systems work. Biophysics seeks to explain biological function in terms of the molecular structures and properties of specific molecules. Because biophysics is a highly interdisciplinary science, it will drive the integration and participation of various departments at WPI. WPI seeks to gain strength in molecular and multi-molecular aspects of biophysics by fostering groups engaged in multidisciplinary research in this field.
Biophysics Focus Area Faculty
Dr. José Arguello (Chemistry and Biochemistry): Arguello’s lab studies the structure and function of membrane transport proteins, in particular bacterial and archaeal heavy metal ATPases, looking at mechanisms of metal selectivity, and their functional role in higher eukaryotes (plants) and symbiotic/pathogenic bacteria. Protein chemistry and molecular biology, along with enzymology and physical methods, are used in these studies.
Dr. Rafael Garcia (Physics): Garcia’s group studies surface and wetting phenomena of biological importance. Studies focus on (a) first-principles predictions of the contact angle of key liquid systems on solid surfaces, with specific attention to the investigation of biologically significant electrostatic and fluctuation-induced forces; (b) understanding the role of boundary conditions on the stress-induced phase transitions occurring in films of proteins or biomemic cell membranes; and (c) the investigation of the effects of surface disorder in confined systems necessary for control, prediction, and/or enhancement of cell/protein film properties.
Dr. Germano Iannacchione (Physics): Iannacchione’s group studies order-disorder phenomena in biomaterials. Using calorimetric, dielectric spectroscopic, and optical microscopy techniques, they study the ordering and self-assembly of biomaterials such as proteins, DNA, and cholesterols. Current work is focused on understanding the elements controlling protein denaturing and folding dynamics, mesoscopic phase behavior of DNA segments, and self-assemblies of filament, tubule, and helical microstructures formed in cholesterol-based model-bile systems.
Dr. George Kaminski (Chemistry and Biochemistry): The Kaminski lab’s focus on computational biophysical chemistry involves producing and applying force fields aimed at increasing accuracy of energies obtained in protein and protein-ligand simulations. The key to this accuracy increase is explicit treatment of many-body interactions. Among the current applications are calculations of protein acidity constants, simulations of farnesyl transferase inhibition, apoptosis simulations, and other projects with the goal of both increasing the level of understanding protein structure and function and making a contribution in the area of cancer research.
Dr. Stephan Koehler (Physics): Koehler’s group investigates soft condensed matter with potential application to self-propulsion. They are studying flow and transport in complex, structured fluids, such as foams and granular media. The goal is to develop continuum-based models and theories based upon measurements. These models in turn will be used to study self-propulsion in complex fluids, such as sand-swimming snakes or micro-organisms moving in two-phase media such as emulsion. They are collaborating with WPI’s robotics enginerering group on building an autonomous sand-swimmer.
Dr. Izabela Stroe (Physics): Stroe’s group studies the thermodynamics and dynamics of proteins and nucleic acids. They are investigating how water affects the structure and stability of proteins, how much water surrounds the biological molecules, how water controls the motion of proteins and nucleic acids, and what the role of water is in protein folding and in DNA transcription. Their toolbox includes unique combinations of dielectric relaxation spectroscopy, relaxation calorimetry, and resonant ultrasound spectroscopy. Answering these questions will lead to a better understanding of protein conformation diseases, to the design-specific inhibitors of undesired protein interactions, and to the ability to rationalize the specific affinity of drugs to misfolded and aggregated proteins.