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Paul Langan will oversee ORNL's research directorate focused on biological and environmental systems science. Credit: ORNL, U.S. Dept. of Energy

Paul Langan will join ORNL in the spring as associate laboratory director for the Biological and Environmental Systems Science Directorate.

A pure lipid membrane formed using lipid-coated water droplets exhibits long-term potentiation, or LTP, associated with learning and memory, emulating hippocampal LTP observed in the brains of mammals and birds. Credit: Jill Hemman/ORNL, U.S. Dept. of Energy

While studying how bio-inspired materials might inform the design of next-generation computers, scientists at ORNL achieved a first-of-its-kind result that could have big implications for both edge computing and human health.

New manufacturing process produces better, cheaper cathodes for lithium-ion batteries. Credit: Andy Sproles/ORNL, U.S. Dept. of Energy

Researchers at ORNL have developed a new method for producing a key component of lithium-ion batteries. The result is a more affordable battery from a faster, less wasteful process that uses less toxic material.

ORNL postdoctoral researcher Runming Tao, pictured with a coin cell battery, led an effort to discover new anode materials for fast-charging lithium-ion batteries. Credit: ORNL/Genevieve Martin, U.S. Dept. of Energy

Researchers at ORNL and the University of Tennessee, Knoxville, discovered a key material needed for fast-charging lithium-ion batteries. The commercially relevant approach opens a potential pathway to improve charging speeds for electric vehicles.

Mars Rover 2020

More than 50 current employees and recent retirees from ORNL received Department of Energy Secretary’s Honor Awards from Secretary Jennifer Granholm in January as part of project teams spanning the national laboratory system. The annual awards recognized 21 teams and three individuals for service and contributions to DOE’s mission and to the benefit of the nation.

Illustration of the intricate organization of the PKA structure, wherein different parts of the protein are connected through elaborate hydrogen bonding networks (dashed yellow lines), glued together by the hydrophobic assemblies (light blue and orange volumes)—all working together to build the functional active site. Insert shows protonation of the transferred phosphoryl group (cyan mesh) and its many interactions with water and the active site amino acid residues. Credit: Jill Hemman/ORNL

OAK RIDGE, Tenn., March 20, 2019—Direct observations of the structure and catalytic mechanism of a prototypical kinase enzyme—protein kinase A or PKA—will provide researchers and drug developers with significantly enhanced abilities to understand and treat fatal diseases and neurological disorders such as cancer, diabetes, and cystic fibrosis.