Fred DydaNational Institute of Diabetes and Digestive and Kidney Diseases (NIDDK), National Institutes of Health (NIH), Bethesda, MD, USA F1000 Faculty Member (since 03 October 2002)
Investigator, Structural Biochemistry Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
BS, Eötvös Lóránd University, Hungary, 1986
PhD, University of Pittsburgh, 1992
The current focus of the lab is to understand the molecular details of mechanisms by which protein activity can be modulated. To function properly, cells must coordinate and choreograph a large number of simultaneous events and processes. These are carried out by proteins. We use X-ray crystallography as our main tool to study the fine details of how the activity and function of protein-protein and protein-DNA complexes are regulated. We employ this approach as it is one of the few experimental techniques that produces high-resolution 'snapshots' to visualize subtle changes in protein structure that often accompany functional regulation. With these snapshots in hand, we use a variety of biochemical, biophysical and simulation approaches to bridge the structures and biological function. For example, we are investigating how the movement of mobile genetic elements such as transposons or viruses is controlled. One of our current areas of emphasis is the Rep protein of adeno-associated virus (AAV); this protein catalyzes the integration of the AAV genome into a specific locus in human chromosome 19, making it an extremely useful tool for gene therapy studies. In addition, we are studying how a ubiquitous group of chaperone proteins known as 14-3-3s are able to direct when and where in a cell to deliver proteins that regulate gene expression.
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F1000 Biology Reports 2010 2:(80) (11 Nov 2010)
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