April 19, 2010

UCSF's Dill to Deliver 53rd Academic Senate Faculty Research Lecture

Ken Dill

The UCSF community is invited today (April 19) to hear Ken Dill deliver the 53rd Faculty Research Lectureship at Mission Bay.

Ken A. Dill, PhD, a professor of pharmaceutical chemistry, biochemistry and biophysics and a national leader in research to clarify and predict the physical properties of proteins and other biological molecules, will deliver the 53rd Faculty Research Lectureship today (April 19).

The Academic Senate selected Dill to present the Faculty Research Lecture, which will take place in Genentech Hall at the Mission Bay campus at 3:30 p.m. A reception will follow. The lecture will be simulcast to Parnassus campus in the School of Nursing, room N 217.

Dill is a professor of pharmaceutical chemistry in UCSF’s School of Pharmacy, and serves as the School’s associate dean for research. He is also a professor of biochemistry and biophysics, and a faculty affiliate in the California Institute for Quantitative Biosciences, headquartered on the UCSF Mission Bay campus.

Dill is a pioneer in theoretical approaches to determine the physical forces that determine the three-dimensional folded shape of proteins. It is this conformation that determines how proteins interact, and knowing this shape is crucial to “rational” design of drugs.
He uses computational techniques and modeling based on statistical mechanics to advance understanding of protein folding. He is also concerned with how amino acid sequences encode the protein structures, and the physical factors that stabilize proteins against unfolding and aggregation - two natural processes that can go awry and cause some of the most serious human diseases, such as Alzheimer’s and Parkinson’s.

Problem Nearly Solved

Dill’s work explained that proteins fold rapidly because of a process of “zipping and assembly,” which resulted in the first physics-based way to predict protein native structures from amino acid sequences. His “Dominant Forces of Protein Folding” has received 2000 citations. In 2008, an editorial in Science magazine declared the protein folding problem now nearly solved and described Dill’s key role in it.

In 1985, Dill developed a computational approach to studying protein principles, called the HP protein model. To date, more than 50 research groups have published on the HP model. This new understanding of the folding code opened the idea of creating foldamers, non-biological molecules that could fold up to have protein-like sequence-structure-function relationships. One such class, called peptoids, is now an active field of research at UCSF and other universities. Some peptoid foldamers research is moving toward clinical trails as lung surfactant mimics, surgical glues for tissue engineering, a new class of antimicrobials, and as potential optical materials. In addition, his modeling has explored questions of early molecular origins of life.

Dill received SB and SM degrees from Massachusetts Institute of Technology, a PhD degree at UC San Diego, and then did postdoctoral work at Stanford University. He was first a professor of chemistry at University of Florida, Gainesville before coming to UCSF in 1989. In 2001, he was appointed associate dean for research at the UCSF School of Pharmacy.

Dill has been elected to the National Academy of Sciences (2008), and is a Fellow of the AAAS, the American Physical Society and the Biophysical Society. He has received the Distinguished Service Award of Biophysical Society (2007) and the Hans Neurath Award of the Protein Society (1998). His textbook, “Molecular Driving Forces,” is used in more than 100 graduate and undergraduate courses.

Problem Nearly Solved

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