Pathways: Routes Through Life, Science, and Protein Folding Are Seldom Straight Lines
Ken Dill is Professor of Chemistry and Physics at Stony Brook University and Director of the Laufer Center for Physical and Quantitative Biology. He received the first Hans Neurath Award in 1998 from the Protein Society for his research on the structures of proteins. He co-founded a coalition of basic research societies that has advocated for bridging the physical and life sciences, and he is a member of the National Academy of Sciences.
Dill explores problems of biological statistical physics, including protein folding, the properties of water, dynamics of small systems, and cell biophysics. He and his colleagues have found that protein folding occurs on funnel-shaped energy landscapes and that protein structures are largely determined by hydrophobic interactions.
Early models of protein folding and biological evolution are envisioned processes that follow linear pathways from beginning to end. But pathways in biology and physics, and in life, are often more random, less directed, less predictable, and more trial-and-error than this. Predicting pathways is also important in other arenas, such as in the enterprise that makes decisions about funding scientific research.