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This story is from the category Pure Research
Date posted: 30/09/2011 Molecular motion in proteins comes in three distinct classes, according to a collaboration by researchers at the Department of Energy's Oak Ridge National Laboratory and the University of Tennessee, in research reported in Physical Review Letters. The research team, directed by ORNL-UT Governor's Chairs Jeremy Smith and Alexei Sokolov, combined high-performance computer simulation with neutron scattering experiments to understand atomic-level motions that underpin the operations of proteins. "The analysis and interpretation of neutron scattering spectra are always difficult for complex molecules such as proteins," said Smith, who directs ORNL's Center for Molecular Biophysics. "We've performed experiments and then shown that simulation can provide a clear view of them. It allows us to see through the complexity and find out what motions are going on." Defining the motions present -- localized diffusion, methyl group rotations and jumps -- is important as it allows scientists to think about how the motions determine the functions of proteins that are critical to all life. "First, we found that experiment and simulation agreed perfectly with each other, which is remarkable," Smith said. "Second, the simulations told us that this type of neutron scattering can be interpreted in a very simple way." See the full Story via external site: www.physorg.com Most recent stories in this category (Pure Research): 04/05/2013: Computer simulations reveal the energy landscape of ion channels |
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