Researchers hope to hijack a natural process called RNA interference to block the production of proteins linked to disease and treat medical conditions for which conventional drugs do not work, including cancer, heart disease, HIV and Parkinson’s disease.
In a new state-of-the-art lab at SLAC National Accelerator Laboratory, components of ribosomes – tiny biological machines that make new proteins and play a vital role in gene expression and antibiotic treatments – form crystals in a liquid solution.
Signs at the lab's entryway warn of the potential for contamination – these delicate samples can be damaged by human touch, a sneeze or a dust particle.
A new screening program will allow researchers to quickly confirm whether precious biological samples yield useful information when struck by the intense X-ray pulses at SLAC's Linac Coherent Light Source (LCLS).
Last year's Nobel Prize in Chemistry – shared by Stanford School of Medicine Professor Brian Kobilka and Robert Lefkowitz of Duke University – recognized groundbreaking research in G protein-coupled receptors (GPCRs). GPCRs are embedded in cell membranes. They interact with signaling molecules outside of cells and trigger responses within cells.
Daniel DePonte, a pioneer in finding ways to serve up a steady and precise supply of crystals, viruses and other precious samples for laser experiments, is the newly hired sample-delivery group leader for SLAC’s Linac Coherent Light Source X-ray laser.
Understanding why proteins interact with certain specific molecules and not with the myriad others in their environment is a major goal of molecular biology. Now, in a series of recent papers, researchers describe how they designed proteins from scratch to have a high affinity and high specificity for targets on flu viruses, and then validated the two best designs using X-ray diffraction data collected at the Stanford Synchrotron Radiation Lightsource (SSRL).