OHSU

Michael Chapman, PH.D.

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Background

Research Interests:

  • Macromolecular structure and function.
  • Virus-host interactions - structural biology of improved gene therapy vectors.
  • Enzymes - dynamics & mechanism.
  • Computational methods - modeling electron microscope images of large complexes.
  • X-ray crystallography, biochemical kinetics, molecular biology.

  • Summary of Current Research

    Michael Chapman is a biophysicist who develops and applies multi-disciplinary approaches to understand viral-host interactions and enzyme mechanism / dynamics. Originally trained as a crystallographer, collaborations allow his research group to combine structural techniques - x-ray diffraction, electron microscopy (EM) & NMR spectroscopy with biochemical kinetics, molecular virology and computational modeling to understand the functional workings of large and dynamic complexes. Dr. Chapman has had a long-standing interest in developing methods to optimize structural models using diverse experimental restraints such as crystallographic maps, EM reconstructions and solid-state NMR, as well as stereochemical restraints from implicit-solvent electrostatics and idealized hydrogen-bonding, experience that will help with Aim 3. He has served in various research/administrative capacities and has mentored 30 graduate students and post-doctoral fellows, many within collaborative projects as proposed here.


    Selected Publications

    "Common hydrogen bond interactions in diverse phosphoryl transfer active sites," PLoS ONE (Vol: 9, Issue: 9, ) - 2014

    "ResLog plots as an empirical metric of the quality of cryo-EM reconstructions," Journal of Structural Biology (Vol: 185, Issue: 3, Page 418-426) - 2014

    "Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs," Protein Science (Vol: 23, Issue: 1, Page 67-75) - 2014

    "Atomic modeling of cryo-electron microscopy reconstructions - Joint refinement of model and imaging parameters," Journal of Structural Biology (Vol: 182, Issue: 1, Page 10-21) - 2013

    "Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form," Biomolecular NMR Assignments ( Page 1-4) - 2013

     

    Contact

      Email Michael Chapman

    503 494-8311

    Memberships & Associations

    Knight Cancer Institute Member