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    <lastmod>2024-01-15</lastmod>
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      <image:title>Academic Research - Hydrogen/Deuterium Exchange Mass Spectrometry (HX-MS)</image:title>
      <image:caption>One particularly powerful chemistry involves hydrogen/deuterium exchange, using heavy water. Imagine a “reagent-less” assay that can track any protein function with residue-level resolution, through backbone dynamics. The method uses bottom-up proteomics concepts, but is not used for complex samples. Can we transform this technology into a truly proteome-competent method?</image:caption>
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      <image:title>Academic Research - Crosslinking Mass Spectrometry (XL-MS)</image:title>
      <image:caption>Chemical crosslinks are like “molecular rulers” that measure distances between two points in (or between) proteins. Conceptually, such measurements could be used to model protein structure and even ultralarge interactomes. How can we install and detect these rulers to support accurate distance measurements in the cell and determine structure of the interactome?</image:caption>
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      <image:title>Academic Research - Covalent Labeling Mass Spectrometry (CL-MS)</image:title>
      <image:caption>A natural complement to HX-MS, this method uses fast-acting chemical reactions to mark protein topography with chemical tags, principally through side-chain labeling. How can we use this versatile approach to probe changes in protein conformation and even support a new method for proximity proteomics?</image:caption>
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      <image:loc>https://images.squarespace-cdn.com/content/v1/620f08c46253c919e6ab8e32/572c39f5-32f2-4ddb-9d88-d87092858c9a/Picture1.png</image:loc>
      <image:title>Academic Research - The Mass Spec Studio</image:title>
      <image:caption>The ultimate software development framework for all structural mass spectrometry applications. The product of 10+ years of effort, the “Studio” has plugins for proteome-scale crosslink detection, automated deuteration analysis and covalent label quantitation, as well as powerful proteomics analysis toolsets. Check it out and join the development team!</image:caption>
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      <image:title>Academic Research - Integrative modeling with multiple data sources</image:title>
      <image:caption>How best should mass spectrometry data be combined with cryo-EM structures, AI models, crystallographic structures and other datasets to generate higher-order structures? We partner with computational biologists to produce accurate, data-driven structures of ultracomplex protein systems.</image:caption>
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      <image:title>Academic Research - End-bridging complex</image:title>
      <image:caption>Eukaryotic cells can repair DNA double strand breaks through a number of mechanisms, including end resection-mediated pathways (like homologous recombination) and non-homologous end-joining (NHEJ). The choice of repair mechanism has an enormous influence over the stability of the genome and thus the development of cancer. How is a given pathway chosen? This is ultimately influenced by higher-order structure. We study these complexes and their regulation with multiple collaborators.</image:caption>
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      <image:title>Academic Research - Non-homologous end joining (NHEJ)</image:title>
      <image:caption>As an example, what proteins comprise the essential complexes for NHEJ, and how are they coordinated to repair lesions in DNA induced by (among other things) ionizing radiation? Building an accurate structural model of this essential repair mechanism is key to understanding an essential biological process and should open up new anticancer therapeutic targets. This is a collaborative project with the lab of Dr. Susan Lees-Miller.</image:caption>
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      <image:title>Academic Research - Mitotic regulation through microtubule dynamics</image:title>
      <image:caption>The mitotic spindle is a structure that forms during cell division and separates duplicated chromosomes. The structure is dominated by dynamic microtubules that engage chromosomes at their centromeres and provide the separation force needed for cell division. Exquisitely complex structures sit a the leading (+) end of microtubules to regulate this behavior. We study how proteins engage the microtubule lattice and adjust their force-generating properties.</image:caption>
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      <image:caption>Professor Department of Biochemistry &amp; Molecular Biology Professor Joint with Oncology, and Physiology &amp; Pharmacology Adjunct Professor Chemistry Member Arnie Charbonneau Cancer Institute Curriculum Vitae</image:caption>
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