About this Event
View mapCIP@Cornell is delighted to host Dr. Joseph A. Loo, Professor in the Department of Biological Chemistry, David Geffen School of Medicine, and in the Department of Chemistry & Biochemistry at the University of California, Los Angeles (UCLA). Dr. Loo is also the Faculty Director of the UCLA Mass Spectrometry and Proteomics Technology Center.
This seminar is sponsored by the Cornell University Biotechnology Resource Center. Light refreshments will be served.
Dr. Loo's talk: "Linking Native Mass Spectrometry to Structural Biology with Top-Down Proteomics"
Native mass spectrometry (MS) of proteins and protein assemblies reveals size and binding stoichiometry. Native MS and native top-down (TD) MS, i.e., fragmentation of the gas-phase protein, can be effective for deriving structural information for soluble and membrane protein complexes, and much of this information can be correlated to the solution-phase structure. We apply these MS tools to address questions related to the growing problem of neurodegenerative diseases (NDs). Alzheimer’s disease is clearly becoming a national health crisis affecting people worldwide; other NDs such as Parkinson’s disease, Huntington’s disease, ALS (Lou Gehrig’s disease), and many others add to the growing healthcare issue for future generations. Protein aggregation, folding/misfolding, modifications, etc all appear to contribute to NDs. Native/top-down MS can be applied to study these factors involved in NDs. Determining the sites of protein binding of potential aggregation-inhibitors may yield clues to the development of therapeutic compounds. Membrane proteins are essential for cellular functions and represent half of drug targets, but they pose a challenge for conventional structure biology methods like X-ray crystallography, cryo-electron microscopy, and nuclear magnetic resonance spectroscopy. Sequence, higher-order structure, and lipid binding for membrane proteins can be characterized by native MS and native TD-MS. TD-MS strategies to identify proteins and complexes on a proteome-scale will be discussed.
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