PO Box 800738
Charlottesville, VA 22908
434-982-6390
Research Areas
The Biophysics Program at the University of Virginia comprises currently 26 faculty who are leaders in their respective fields. The program is particularly strong in the following areas of research in Molecular and Cell Biophysics:
Structural Biology & Structural Genomics
Structural Biology of Membrane Proteins & Membrane Biophysics
Spectroscopy & Thermodynamics of Macromolecular Interactions
and High Resolution Imaging & Cell Biophysics
Structural Biology
&
Structural Genomics
The University has made special efforts in the past 10 years to build a very strong program in structural biology. The Medical School has hired 5 new faculty members in macromolecular X-ray crystallography and equipped these new laboratories with state-of-the-art diffractometers and other equipment. These laboratories work on subjects ranging from the elucidation of structures of enzymes involved in signal transduction, hormone receptors, membrane proteins, as well as on improving methods for X-ray data collection and processing. The most preeminent software package used for macromolecular crystallographic data collection at synchrotrons world-wide has been developed by a faculty member at UVa. NMR spectroscopy has undergone a similar expansion at UVa in the last 3 years. Current NMR laboratories are located in the Departments of Chemistry, Molecular Physiology and Biological Physics, as well as Biochemistry and Molecular Genetics. Facilities include two 600 MHz, two 500 MHz, one 360 MHz, a 300 MHz machine equipped with high power probes for solids, as well as other experimental NMR spectrometers. Topics that are currently investigated by faculty members of the program using NMR spectroscopy include structure determinations of DNA binding proteins that are important in leukemia, domains playing a critical role in episenetics, as well as membrane proteins. The internal dynamics of proteins are being investigated and new contrast agents for magnetic resonance imaging are being developed. Other tools used by structural biologists at UVa are electron and atomic force microscopes, often coupled with computerized image reconstruction techniques from periodic arrays or filaments. Two field-emission gun electron microscopes and several AFMs, including one that works at cryogenic temperatures and that was developed at UVa, are operated by biophysicists at UVa. The structures of actin filaments and protein-DNA complexes are investigated by cryo-EM, and various membrane and other proteins are studied by AFM.
Click here for a list of faculty members conducting research in this area.
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Structural Biology
of Membrane Proteins
&
Membrane Biophysics
The study of the dynamic structure of membranes has been one of the traditional strengths of the Biophysics program at the University of Virginia. Seminal contributions to the structure and thermodynamic stability of and lipid interactions in lipid bilayers have been made at UVa since the late 1960s. These studies included some of the earliest contributions to our current understanding of lipid domains and interactions of cholesterol in cell membranes - a topic that has recently raised renewed interest among cell biologists and biophysicists alike. Many new faculty have been hired in this area. While a strong interest in membrane lipids and particularly their interactions with membrane proteins persists, new faculty expertise has been added in the area of membrane protein structure and function. Structures of membrane proteins are being studied by X-ray crystallography, NMR and EPR spectroscopy, and by AFM. The concentration of so many different techniques to study structures of membrane proteins is unique at the University of Virginia. Systems investigated include ion channels, ATP-driven ion pumps, toxins, C2 and other domains of membrane-interactive proteins that are important in signal transduction, and membrane fusion proteins. Besides magnetic resonance, crystallography and AFM, various other spectroscopies and imaging techniques, as well as electrophysiological, thermodynamic, and single molecule techniques are employed in the various laboratories.
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Spectroscopy
&
Thermodynamics
of
Macromolecular Interactions
Faculty of the Biophysics program at UVa use and develop a large variety of spectroscopic techniques to answer biophysical problems. NMR spectroscopy is used not only to solve the structures of macromolecules and their interactions with DNA or membrane lipids, but also to study fundamental aspects of the dynamics of water at macromolecular interfaces and how macromolecular motions are affected by solvent and physiologically important ligand interactions. Special equipment has been developed at UVa for some of these studies. Site-directed spin-labeling has become a powerful tool to study the structure and interactions of proteins, particularly membrane proteins by EPR spectroscopy. Two laboratories at UVa pursue such studies. Fourier transform infrared (FTIR), fluorescence, and circular dichroism (CD) spectroscopy are used by several laboratories on a routine basis. In some cases new applications are being developed. Protein folding is studied in two laboratories by various spectroscopic, thermodynamic, and kinetic techniques.
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High Resolution Imaging
&
Cell Biophysics
Imaging systems using electrons, photons, or inter-molecular forces are used and developed by faculty of the Biophysics program at UVa. Two FEG electron microscopes (one state-of-the-art cryo-FEG EM was installed in 2000) are used to study, at the highest resolution, the structures of proteins interacting with DNA, membrane proteins, actin, and actomyosin filaments. Several other EMs with conventional electron sources are also used by these investigators. The structures of smooth muscle cells are compositionally analyzed by electron energy loss spectroscopy (EELS) and confocal optical microscopes are used to study morphological changes in normal and transformed cells. Total internal reflection fluorescence microscopy is used to measure the binding and interactions of proteins at membrane surfaces. One laboratory at the University of Virginia has made ground-breaking progress in the use of AFM for imaging biological specimens in physiological solutions and at cryogenic temperatures.
Click here for a list of faculty members conducting research in this area.
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© 2008 by the Rector and Visitors of the University of Virginia
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