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: Novel Ion Channel Design Using Lipids

Ion permeation in P2X receptor

image size: 792.2KB
made with VMD

ATP, a ubiquitously prevalent biomolecule, which is best known for being the principal energy source for a living cell, also plays a crucial role in inter-cellular communication, thus acting as a signaling molecule. One of the major receptors in this signaling cascade are the P2X receptors which are trimeric, non-selective cation channel activated by ATP and responsible for key processes such as muscle contraction, inflammatory response, pain, and even taste signal transduction. As a result of their extensive prevalence and important implications in human physiology, P2X receptors serve as important pharmacological targets for cardiovascular, neuronal, and inflammatory diseases. In a recent collaborative study with experimental structural biologists, molecular dynamics simulations of a membrane-embedded model of a P2X receptor performed with NAMD were used to reveal intricate details of the ion permeation mechanism and pathway. Surprisingly, it was observed that one half of the ion permeation pathway is composed of lipids on one side and of the protein residues on the other side, a novel design for an ion translocation pore. The study demonstrates yet another active functional role for lipids in membrane protein function, further emphasizing the importance of lipid protein interactions in biological processes. More details can be found here.

The Future of Biomolecular Modeling

A 2015 TCBG Symposium brought together scientists from across the Midwest to brainstorm about what's on the horizon for computational modeling. See a summary of what these experts foresee. Read more

Quantum Biology and Polyenes-When Theorists and Experimentalists Unite

Starting with a discovery at Harvard in 1971 of a hidden state, Klaus Schulten spent a large portion of his career demystifying the polyenes, versatile molecules central to vision and photosynthesis. By Lisa Pollack. Read more


Hybrid QM/MM calculations now available in NAMD 2.12Hands-on Workshop on Computational Biophysics at Urbana, ILResearchers solve the atomic structure of stalled ribosomeNAMD 2.12 is released


Juan Perilla, Postdoctoral Associate


  • 06 Mar 2017 - Christopher Cooper
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