Precision mirrors to focus X-rays and neutron beams could speed the path to new materials and perhaps help explain why computers, cell phones and satellites go on the blink.
In the last few years, a team led by Gene Ice of the Department of Energys Oak Ridge National Laboratory has improved by a factor of nearly 10 the performance of mirrors that enable researchers to examine variations in structure and chemistry and even individual nanoparticles. Information at this fine level is essential to understanding composition and structure of materials, and researchers continue to push the boundaries.
"Theres a worldwide race to develop high-performance mirrors that will dramatically expand the capabilities of major science facilities like the Advanced Photon Source and the Spallation Neutron Source," said Ice, a member of ORNLs Metals & Ceramics Division. "We are now able to see in far greater detail the three-dimensional heterogeneous - or dissimilar -- structure of materials and study internal interactions of one nanoparticle next to another."
Ron Walli | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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