For years, the comparison of simulated and experimental protein folding kinetics has been a "Holy Grail" for biologists and chemists. But scientists seeking to confirm protein-folding theory with laboratory experiments have been unable to cross the microsecond barrier. This obstacle in time existed because experiments could not be performed fast enough, nor simulations run long enough, to permit a direct comparison.
Now, measurements from the University of Illinois at Urbana-Champaign and molecular dynamics simulations from Stanford University have at last been compared and found to be in very good agreement. A paper describing the work has been accepted for publication in the journal Nature, and was posted on its Web site www.nature.com/nature.
"By crossing the microsecond barrier, we can directly compare simulated and experimental protein folding dynamics, such as folding rates and equilibrium constants," said Martin Gruebele, an Illinois professor of chemistry, physics and biophysics.
James E. Kloeppel | EurekAlert!
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