Berkeley Center for Structural Biology (BCSB) beamlines 5.0.2, 8.2.1, and 8.2.2 at the Advanced Light Source (ALS) were used to experimentally verify de novo protein structures designed by citizen scientists playing the computer game Foldit.
A Frog Worth Kissing: Natural Defense Against Red Tide Toxin Found in Bullfrogs
A team led by Berkeley Lab faculty biochemist Daniel Minor has discovered how a protein produced by bullfrogs binds to and inhibits the action of saxitoxin, the deadly neurotoxin made by cyanobacteria and dinoflagellates that causes paralytic shellfish poisoning. The findings, published this week inĀ Science Advances, could lead to the first-ever antidote for the compound, which blocks nerve signaling in animal muscles, causing death by asphyxiation when consumed in sufficient quantities.
X-ray Footprinting Reveals Molecular Basis of Orange Carotenoid Protein Photoprotection
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.
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.
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.
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