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"This also represents a big step forward in our efforts to create computational simulations of biological processes," Yang said. "In this case, we first made a prediction of the enzyme structure via computer and later verified it through direct observation in a laboratory, rather than the other way around. This is a most unusual accomplishment, and one that indicates we are becoming more advanced in our ability to answer questions relating to biological functions at the molecular level."

"Because of the key role that IMPDH plays, scientists have focused on developing new antiparasitic drugs that target it," Yang said. "Our research will certainly contribute to this process."

Joseph Schlenoff, the chairman of FSU's Department of Chemistry and Biochemistry, praised Yang's computational methods as "extremely powerful because they are rigorous, make few assumptions and approximate the complexity of the real world. The accurate predictions that result represent success that has been promised to us for so long by scientists using computers."

Collaborating with Yang on the project were Gavin J.P. Naylor, an associate professor in FSU's Department of Scientific Computing; Donghong Min, a postdoctoral associate in the Institute of Molecular Physics; Hongzhi Li, a former postdoc in the Institute of Molecular Physics; Clemens Lakner, a graduate assistant in the Department of Biological Science; David Swofford, a research scientist at Duke University and former FSU faculty member; Lizbeth Hedstrom, a professor of biochemistry at Brandeis University; and postdocs Helen R. Josephine and Iaian S. MacPherson, both of Brandeis.

Together the researchers wrote about their findings in a paper, "An Enzymatic Atavist Revealed in Dual Pathways for Water Activation," that was published this summer in
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