Search NASA⌕ Search

Engineering topics

Williams, Jonathan K.

Publications and source records attributed to Williams, Jonathan K..

F2D2 Targetry Overview and Conceptual Design Updates

F2D2 is a proposed 2.5 MW beam dump facility using PIP-II beam to serve dark sector physics experiments, and potentially other users. Further updates to the conceptual design are presented, along with targetry theory informing the design.

43 PARTICLE ACCELERATORS↗

The Fermilab Facility for Dark Matter Discovery (F2D2): A Conceptual PIP-II Beam Stop Facility for Dark Sector Physics

What do the accelerator target stations of the next decade look like? The NuMI beamline, fed by Fermilab s Main Injector, recently exceeded 1 MW beam power. Future experiments fed by the PIP-II superconducting linear accelerator might demand upwards of 2 MW in continuous-wave mode, compared to the pulsed beams typical of neutrino experiments. Looking further into the future, the Muon Collider front end includes a target station with even higher power 5 MW or beyond. How do we build a 2+ MW target facility? How does a high-power, low-energy, CW beam affect target design compared to conventional high-energy neutrino targets? How do we manage radiation and heat? How is the facility serviced? What is the current state of capability, and what technologies do we need to develop? These questions are answered in the context of F2D2, a conceptual target station design for dark sector physics experiments using beam from PIP-II.

Williams, Jonathan K.↗

Evolution of the SARS-CoV -2 proteome in three dimensions (3D) during the first 6 months of the COVID -19 pandemic

Understanding the molecular evolution of the SARS-CoV-2 virus as it continues to spread in communities around the globe is important for mitigation and future pandemic preparedness. Three-dimensional structures of SARS-CoV-2 proteins and those of other coronavirusess archived in the Protein Data Bank were used to analyze viral proteome evolution during the first 6 months of the COVID-19 pandemic. Analyses of spatial locations, chemical properties, and structural and energetic impacts of the observed amino acid changes in >48 000 viral isolates revealed how each one of 29 viral proteins have undergone amino acid changes. Catalytic residues in active sites and binding residues in protein–protein interfaces showed modest, but significant, numbers of substitutions, highlighting the mutational robustness of the viral proteome. Energetics calculations showed that the impact of substitutions on the thermodynamic stability of the proteome follows a universal bi-Gaussian distribution. Here detailed results are presented for potential drug discovery targets and the four structural proteins that comprise the virion, highlighting substitutions with the potential to impact protein structure, enzyme activity, and protein–protein and protein–nucleic acid interfaces. Characterizing the evolution of the virus in three dimensions provides testable insights into viral protein function and should aid in structure-based drug discovery efforts as well as the prospective identification of amino acid substitutions with potential for drug resistance.

59 BASIC BIOLOGICAL SCIENCES↗