The European Molecular Biology Organization (EMBO) has elected Molecular Biophysics and Integrated Bioimaging (MBIB) senior faculty scientist Eva Nogales as an associate member. The organization of more than 1,800 leading researchers promotes excellence in the life sciences in Europe and beyond. Nogales, who is also a Howard Hughes Medical Institute (HHMI) investigator and professor at UC Berkeley, is among 56 new members and associate members EMBO will formally welcome at the annual meeting in Heidelberg, Germany, in October 2019.
Breakthrough in Membrane-Protein Design Settles Long-Standing Debate
Membrane proteins that connect a cell’s inner workings with the outside world are essential for life and genetic mutations that affect their structural integrity or biological function are the cause of many diseases. Given their importance, researchers are interested in ascertaining the general physics principles underlying how membrane proteins fold and stabilize their molecular structures. Using high-resolution protein crystallography at the Advanced Light Source (ALS) Beamline 8.3.1, scientists from UCSF characterized designed membrane proteins to better understand the forces that stabilize these large, complex structures.
Read the ALS Science Highlight.
PhyloChip Provides Clarity Amid Hawaiian Water Contamination Concerns
To better understand the cause of high counts of potentially pathogenic fecal indicator bacteria (FIB) in the watersheds of the Mahaulepu Valley and Waikomo Stream in southeast Kauai, the Hawaii Department of Health (DOH) commissioned a study by Berkeley Lab microbial ecologists Gary Andersen and Eric Dubinsky. The duo is frequently invited to lead microbial water assessment projects thanks to their expertise and the PhyloChip, a credit card-sized microbial detection technology invented by Andersen and others at Berkeley Lab.
SIBYLS Sheds Light on Enzyme that Regulates Blood-clotting Factor
A group of researchers at Washington University School of Medicine have used the capabilities available at the Advanced Light Source’s SIBYLS beamline to gain insight into an enzyme that functions in blood clotting. ADAMTS13, which stands for a disintegrin and metalloproteinase with thrombospondin-1 repeats, member 13, is a multi-domain protease enzyme whose catalytic mechanism involves a metal. It is the only known protein to regulate the adhesive function of von Willebrand factor (VWF), a blood clotting protein involved in hemostasis.
BCSB Helps Elucidate Mechanism of Innate Immune Response
The crystallographic study of STING (stimulator of interferon genes), a transmembrane protein that plays a key role in innate immunity, in complex with TBK1 (serine/threonine-protein kinase), an enzyme that regulates the inflammatory response to foreign DNA, is extremely challenging due to weakly diffracting crystals. But thanks to the expertise of Berkeley Center for Structural Biology (BCSB) scientists, researchers from Texas A&M University (TAMU) were able to pinpoint the conserved motif of STING that mediates the recruitment and activation of TBK1. They published their results in Nature.
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