Remembering Klaus Schulten

“When I was a young man, my goal was to look with mathematical and computational means at the inside of cells, one atom at a time, to decipher how living systems work. That is what I strived for and I never deflected from this goal.”

Klaus Schulten, professor of physics and Beckman Institute faculty member for nearly 25 years, has died after an illness. Schulten, who led the Theoretical and Computational Biophysics Group, was a leader in the field of biophysics, conducting seminal work in the area of molecular dynamics simulations, illuminating biological processes and structures in ways that weren’t possible before. His research focused on the structure and function of supramolecular systems in the living cell, and on the development of non-equilibrium statistical mechanical descriptions and efficient computing tools for structural biology. Schulten received his Ph.D. from Harvard University in 1974. At Illinois, he was Swanlund Professor of Physics and was affiliated with the Department of Chemistry as well as with the Center for Biophysics and Computational Biology; he was Director of the Biomedical Technology Research Center for Macromolecular Modeling and Bioinformatics as well as Co-Director of the Center for the Physics of Living Cells.


A memorial service and reception was held November 7. The Beckman Institute will host an honorary symposium in 2017.




Highlights of our Work

Highlight: A Molecular Shuttle

bc1 complex embedded in membrane

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Photosynthetic organisms have been optimized by over two billion years of evolution into energy-harvesting machines that surpass the efficiency of man-made solar devices. Employing a network of hundreds of proteins, these organisms transform energy from the incident sunlight into ATP molecules - the universal fuel for sustaining cellular activities. A key step in the conversion of solar energy into ATP involves shuttling of negative charges or electrons between widely separated sites on the cell membrane. This membrane-wide charge transportation is accomplished by the cytochrome c family of proteins. Cytochrome c finds and docks to an electron donor protein, accepts the electron and unbinds as a result of it, and afterwards finds an electron acceptor protein, docks to it to deliver the electron and unbinds to repeat the sequence. Given its ubiquitous role in photosynthesis and respiration, the recognition, binding and unbinding mechanism of cytochrome c have been a focus of intense biochemical investigations over the past three decades. However, little is deciphered on the details of cytochrome c activity. A recent study based on molecular dynamics simulations with NAMD reveals the working principles of cytochrome c in atomic resolution. The calculations suggest that electrostatic forces drive the cytochrome c binding, and enable membrane-wide electron transfer. More about the cytochrome c protein can be found here.
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VMD 1.9.3 is releasedTajkhorshid, TCB faculty, along with two other UIUC professors receive The High-Risk, High-Reward Research (HRHR) program supported by the NIH

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