Filter News
Area of Research
- (-) Biology and Environment (3)
- (-) National Security (3)
- (-) Neutron Science (6)
- Advanced Manufacturing (1)
- Clean Energy (10)
- Computational Engineering (1)
- Computer Science (2)
- Fusion and Fission (1)
- Isotopes (1)
- Materials (12)
- Materials for Computing (2)
- Quantum information Science (1)
- Supercomputing (16)
News Topics
- (-) Artificial Intelligence (1)
- (-) Bioenergy (2)
- (-) Biomedical (2)
- (-) Computer Science (3)
- (-) Machine Learning (1)
- (-) Materials Science (3)
- (-) Security (1)
- 3-D Printing/Advanced Manufacturing (1)
- Biology (4)
- Biotechnology (1)
- Chemical Sciences (1)
- Climate Change (1)
- Composites (1)
- Coronavirus (1)
- Cybersecurity (2)
- Environment (3)
- Fusion (1)
- Materials (2)
- Microscopy (1)
- Nanotechnology (2)
- National Security (1)
- Neutron Science (12)
- Physics (2)
- Polymers (1)
- Quantum Science (1)
- Sustainable Energy (1)
Media Contacts
![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](/sites/default/files/styles/list_page_thumbnail/public/2019-03/19-G00204_MR_graphic_Kovalevsky_proof5_2.png?h=b7fbb1a9&itok=wrZFNX-o)
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.