Ken A. Dill

Dr. Dill performs research at the interface between statistical physics and biology, at the level of biomolecules and cells.  He studies the physics of how proteins fold, the microscopic origins of the unusual physical properties of water, and the foundations of non-equilibrium statistical physics. 

At the University of California, San Francisco from 1983 through 2010, he elucidated the underlying physical properties of how protein molecules fold into their biological shapes.  Dr Dill's foundational 1985 paper proposed two key ideas.  First, he showed that the dominant component of the "folding code" was the binary patterning of hydrophobic and polar subunits.  Experimental work subsequently confirmed the theory. Dr Dill's highly cited 1990 article, "Dominant Forces in Protein Folding" Biochemistry 29 (31), 7133-7155 made his insights accessible to a broad community of scholars from biology, physics, and chemistry. 

Second, he showed that protein folding takes place on funnel-shaped energy landscapes (see, From Levinthal to pathways to funnels. Nature Structural Biology 1997 4(10), 10-19). Today, folding funnels and energy landscapes are concepts that dominate the field. Moreover, the insight that principles underlying folding patterns among proteins should extend beyond biopolymers led to a large new research field on synthetic foldamers including peptoids, one class of non-natural heteropolymers.

Since 2010, Dr Dill has been the Director of the Laufer Center for Physical & Quantitative Biology, at Stony Brook University on Long Island, NY. Dr. Dill oversees collaborative research that aims to advance biology and medicine through discoveries in physics, mathematics and computational science. Dr. Dill and other researchers at the Center study the biochemical networks in cells and use computational models to learn more about cells and their processes in biology and in diseases.

His recent work has led to insights about how the laws of physics constrain and enable the biological properties and evolution of cells. His findings suggest that natural selection acts not only on individual genes and biomolecules, but also on the physical properties and large classes of proteins at a time.