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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.

Oak Ridge National Laboratory’s Leah Broussard shows a neutron-absorbing "wall" that stops all neutrons but in theory would allow hypothetical mirror neutrons to pass through. Credit: Genevieve Martin/ORNL, U.S. Dept. of Energy

To solve a long-standing puzzle about how long a neutron can “live” outside an atomic nucleus, physicists entertained a wild but testable theory positing the existence of a right-handed version of our left-handed universe.

Illustration of the optimized zeolite catalyst, or NbAlS-1, which enables a highly efficient chemical reaction to create butene, a renewable source of energy, without expending high amounts of energy for the conversion. Credit: Jill Hemman, Oak Ridge National Laboratory/U.S. Dept. of Energy

Illustration of the optimized zeolite catalyst, or NbAlS-1, which enables a highly efficient chemical reaction to create butene, a renewable source of energy, without expending high amounts of energy for the conversion. Credit: Jill Hemman, Oak Ridge National Laboratory/U.S. Dept. of Energy

Catherine Schuman during Hour of Code

ORNL computer scientist Catherine Schuman returned to her alma mater, Harriman High School, to lead Hour of Code activities and talk to students about her job as a researcher.

Snowflakes indicate phases of super-cold ice

An ORNL-led team's observation of certain crystalline ice phases challenges accepted theories about super-cooled water and non-crystalline ice. Their findings, reported in the journal Nature, will also lead to better understanding of ice and its various phases found on other planets, moons and elsewhere in space.

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.