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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.

The students analyzed diatom images like this one to compare wild and genetically modified strains of these organisms. Credit: Alison Pawlicki/Oak Ridge National Laboratory, US Department of Energy.

Students often participate in internships and receive formal training in their chosen career fields during college, but some pursue professional development opportunities even earlier.

Materials—Engineering heat transport

Scientists have discovered a way to alter heat transport in thermoelectric materials, a finding that may ultimately improve energy efficiency as the materials

Strain-tolerant, triangular, monolayer crystals of WS2 were grown on SiO2 substrates patterned with donut-shaped pillars, as shown in scanning electron microscope (bottom) and atomic force microscope (middle) image elements.

A team led by scientists at the Department of Energy’s Oak Ridge National Laboratory explored how atomically thin two-dimensional (2D) crystals can grow over 3D objects and how the curvature of those objects can stretch and strain the 

Pictured in this early conceptual drawing, the Translational Research Capability planned for Oak Ridge National Laboratory will follow the design of research facilities constructed during the laboratory’s modernization campaign.

OAK RIDGE, Tenn., May 7, 2019—Energy Secretary Rick Perry, Congressman Chuck Fleischmann and lab officials today broke ground on a multipurpose research facility that will provide state-of-the-art laboratory space 

ORNL researcher Karren More has been elected fellow of the Microscopy Society of America.

OAK RIDGE, Tenn., March 22, 2019 – Karren Leslie More, a researcher at the Department of Energy’s Oak Ridge National Laboratory, has been elected fellow of the Microscopy Society of America (MSA) professional organization.

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.

Neutron scattering allowed direct observation of how aurein induces lateral segregation in the bacteria membranes, which creates instability in the membrane structure. This instability causes the membranes to fail, making harmful bacteria less effective.

As the rise of antibiotic-resistant bacteria known as superbugs threatens public health, Oak Ridge National Laboratory’s Shuo Qian and Veerendra Sharma from the Bhaba Atomic Research Centre in India are using neutron scattering to study how an antibacterial peptide interacts with and fights harmful bacteria.

To develop complex materials with superior properties, Vera Bocharova uses diverse methods including broadband dielectric spectroscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy; photographer Jason Richards

Vera Bocharova at the Department of Energy’s Oak Ridge National Laboratory investigates the structure and dynamics of soft materials—polymer nanocomposites, polymer electrolytes and biological macromolecules—to advance materials and technologies for energy, medicine and other applications.

ORNL alanine_graphic.jpg

OAK RIDGE, Tenn., Jan. 31, 2019—A new electron microscopy technique that detects the subtle changes in the weight of proteins at the nanoscale—while keeping the sample intact—could open a new pathway for deeper, more comprehensive studies of the basic building blocks of life.