MBIB News

Research led by UC Berkeley scientists found that adults who reported a decline in sleep quality in midlife (40s–60s) had more beta amyloid and tau clusters in their brains—both of which are associated with a higher risk of developing dementia later in life. The same study also revealed that people with high levels of tau protein in their brains were more likely to lack the synchronized brain waves that are crucial to getting a good night’s sleep. Together, the findings suggest that sleep changes detectable in a simple overnight sleep study may serve as biomarkers for later risk of dementia.

Researchers at Berkeley Lab and Michigan State University (MSU), led by Corie Ralston and Cheryl Kerfeld, performed X-ray footprinting mass spectrometry (XFMS) experiments at the Advanced Light Source (ALS) beamline 5.3.1, which revealed new mechanistic details of the key events in orange carotenoid protein (OCP) photoprotection. XFMS is ideally suited to probing conformational dynamics at the single residue level, providing both a spatial and temporal view of site-specific changes in the OCP and its interaction with the fluorescence recovery protein (FRP). The experiments showed that FRP provides an extended binding region that holds the OCP together and forces proximity of the two domains that accelerate relaxation of OCP to its native state.

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.

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.

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.