High Flux Isotope Reactor a fit for Nobel laureate’s designer proteins

Science today brings solutions tomorrow

The ability to design proteins also opens doors for a range of other applications, such as streamlined vaccine development, a greener chemical industry and new nanomaterials. And since most enzymes are proteins, Baker’s work can also help improve everything from drug design to biofuel production, plastic decomposition and more.

“Biology holds enormous promise for life-saving breakthroughs and new technologies, and those discoveries will be possible in large part thanks to powerful research tools like HFIR,” ORNL Director Stephen Streiffer said. “It’s edifying to see this foundational ORNL capability, neutron scattering — which earned its own Nobel Prize in Physics — contribute to the work of new Nobel laureates. This is also a testament to HFIR’s long-standing and critical role across decades. Researchers who are leading new innovations can come to HFIR for answers.” 

Baker relies primarily on advanced computing for protein structure design. Since the early 2000s, Baker, with the help of his research team based at the University of Washington, has been curating a databank, which now includes more than 200,000 protein structures he uses to create new proteins to help develop new medicines.

“David Baker used ORNL’s neutron scattering facilities to study hydrogen locations and bonds of his designer protein. It is, of course, fantastic and very rewarding to see scientific work recognized by the Nobel committee, and we are proud to have contributed to some of his studies with HFIR,” said Jens Dilling, associate laboratory director for Neutron Sciences at ORNL.

The June workshop, “Neutrons in Structural Biology,” held in Arlington, Virginia, provided a venue for structural biology and biochemistry experts, such as from Baker’s lab, early career researchers, and students to discuss scientific advances and collaboration opportunities, with an emphasis on new capabilities planned for ORNL’s Second Target Station (STS) at the Spallation Neutron Source (SNS). Instruments proposed for the STS will be capable of performing biological neutron crystallography on more complex systems than are possible today. SNS is the nation’s leading source of pulsed neutron beams for research.

“We cannot reliably predict where active hydrogen atoms sit and how chemistry is performed in many of these systems, which is why our biology user groups come to ORNL to use neutrons,” Myles said. “Workshops like this reconfirm for us how unique and in demand neutrons are, showcasing the power of neutrons in scientific discovery.”

Myles leads an IMAGINE research team funded by DOE’s Biopreparedness Research Virtual Environment (BRaVE) initiative, a program that bolsters DOE’s strategy for general biopreparedness and response to biological threats. Myles and his team have also designed an upgrade for IMAGINE that will enhance neutron analyses to collect data from radically smaller protein crystals, enabling faster therapeutic drug development. The upgrade increases signals from hydrogen atoms, making key features in protein structures more visible for efficient characterization. 

HFIR is a DOE Office of Science user facility.

UT-Battelle manages ORNL for DOE’s Office of Science, the single largest supporter of basic research in the physical sciences in the United States. The Office of Science is working to address some of the most pressing challenges of our time. For more information, visit energy.gov/science. — Sumner Brown Gibbs

This Oak Ridge National Laboratory news article "High Flux Isotope Reactor a fit for Nobel laureate’s designer proteins" was originally found on https://www.ornl.gov/news

 

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