Bier conducted his studies using a top-down approach of the intact complex using a cryodetector-based MALDI TOF mass spectrometer (Macromizer) equipped with 16 superconducting tunnel junctions. Carnegie Mellon houses the only two of these instruments in the U.S. Biers group can use the Macromizer to measure the molecular weight of a large, intact protein or a protein complex in a matter of seconds. Because it can measure intact protein complexes, this approach also avoids the sample loss that typically occurs during the bottom-up approach.
Our results are a first step toward our ultimate goal to identify a virus, clotting factor or any type of large biological molecule by just weighing it or its gas-phase-generated fragments, said Bier. This would provide a rapid clinical tool to diagnose a viral infection or a blood disease, for example.
Bier is collaborating with Roger Hendrix, a professor of biological sciences at the University of Pittsburgh, who studies how the outer shell of the HK97 virus assembles. Because Hendrix characterizes viral proteins, particles and subunits that are too heavy to study using currently available mass spectrometers, Bier hopes that his data will help them discover new biology. Bier is also collaborating with Dominic Chung, a research professor in the Department of Biochemistry at the University of Washington in Seattle, and Tom Howard, a medical doctor at the VA Greater Los Angeles Healthcare System, who together study von Willebrand factors.
Marks analysis by mass spectrometry displays a lot
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| Contact: Amy Pavlak apavlak@andrew.cmu.edu 412-268-8619 Carnegie Mellon University Source:Eurekalert |