Edward H. Egelman

Started on January, 1999
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I am a biophysicist known for my work on the structure and function of protein and nucleoprotein polymers. I developed the algorithm that is now widely used in cryo-electron microscopy for the three-dimensional reconstruction of helical filaments and tubes. My research has ranged from studies of actin to bacterial pili to viruses that infect hosts living in nearly boiling acid. I was born in New York and graduated from Brandeis University in 1976 with a B.A. in physics. I started as a Ph.D. student in experimental high energy physics at Harvard, but changed fields and received my Ph.D. from Brandeis University in 1982 in biophysics. I was a Jane Coffin Childs postdoctoral fellow at the Medical Research Council Laboratory of Molecular Biology in Cambridge, UK, and became an Assistant Professor at Yale University in 1984. In 1989 I moved to the University of Minnesota where I was an Associate and Full Professor, and in 1999 moved to the University of Virginia where I am now a Harrison Distinguished Professor. I have been president of the Biophysical Society and Editor-in-Chief of Biophysical Journal, and am a Fellow of both the Biophysical Society and the American Academy of Microbiology. In 2019 I was elected to the National Academy of Sciences.

Research Interests

The Egelman laboratory uses structural biology to understand the function and evolution of protein and nucleoprotein polymers. The main method employed is cryo-electron microscopy, which now allows for near-atomic resolution of biological polymers almost routinely. While I started as a graduate student looking at F-actin, the methods I helped develop have allowed for high resolution structural studies of many other polymers. I have been working on pili of pathogenic bacteria, which are an essential virulence factor. What has been surprising is that small numbers of amino acid changes can lead to large variations in quaternary structure, something that I have termed the lability of quaternary structure. This can be seen as a mechanism in evolution for the amplification of relatively small numbers of substitutions in the primary sequence of proteins. I have gone on using in vitro systems with peptides to show how dramatic these changes in quaternary structure can be. My laboratory has also been interested in protein polymers that resist the most extreme environments, such as pili on the surface of archaea that live in nearly boiling acid. Our studies of viruses that infect such hyperthermophilic acidophiles have revealed a packing of DNA in the A-form which appears to afford protection against such harsh conditions.