Filter News
Area of Research
- (-) Neutron Science (22)
- Advanced Manufacturing (1)
- Biology and Environment (12)
- Clean Energy (36)
- Computational Engineering (1)
- Computer Science (4)
- Fusion and Fission (4)
- Isotope Development and Production (1)
- Isotopes (2)
- Materials (55)
- Materials Characterization (1)
- Materials for Computing (6)
- Materials Under Extremes (1)
- National Security (10)
- Nuclear Science and Technology (2)
- Quantum information Science (1)
- Sensors and Controls (1)
- Supercomputing (32)
News Topics
- (-) Artificial Intelligence (1)
- (-) Biomedical (4)
- (-) Energy Storage (2)
- (-) Materials Science (13)
- (-) Quantum Science (4)
- (-) Security (1)
- 3-D Printing/Advanced Manufacturing (3)
- Big Data (1)
- Bioenergy (3)
- Biology (4)
- Biotechnology (1)
- Climate Change (1)
- Composites (1)
- Computer Science (6)
- Coronavirus (5)
- Cybersecurity (1)
- Decarbonization (1)
- Environment (3)
- Frontier (1)
- Fusion (1)
- High-Performance Computing (1)
- Materials (6)
- Microscopy (1)
- Nanotechnology (6)
- National Security (1)
- Neutron Science (40)
- Nuclear Energy (1)
- Physics (7)
- Space Exploration (1)
- Summit (4)
- Sustainable Energy (2)
- Transportation (2)
Media Contacts
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.
For more than 50 years, scientists have debated what turns particular oxide insulators, in which electrons barely move, into metals, in which electrons flow freely.