Tobias W Giessen
Assistant Professor of Biological Chemistry
[email protected]

Available to mentor

Tobias W Giessen
Assistant Professor
  • About
  • Links
  • Qualifications
  • Recent Publications
  • About

    The Giessen Lab is interested in the structure, function, and engineering of protein organelles, protein machines, and enzyme filaments. Our current focus lies on microbial protein organelles, compartments, and filaments involved in detoxification, nutrient utilization, and natural product biosynthesis, as well as on the discovery and characterization of novel enzyme machines and assemblies involved in the biosynthesis of bioactive compounds. We endeavor to leverage our molecular level insights into large protein assemblies for synthetic biology applications in drug delivery, biocatalysis, and bionanotechnology. Our interdisciplinary work utilizes techniques and approaches spanning the fields of biochemistry, structural biology (cryo-EM and x-ray crystallography), microbiology and synthetic biology.

    Links
    • Giessen Lab Website
    • Tobias W. Giessen - Google Scholar
    Qualifications
    • Postdoctoral Research Fellow
      Harvard Medical School | Wyss Institute for Biologically Inspired Engineering at Harvard, Systems Biology, 2018
    • Postdoctoral Research Fellow
      Loewe Center for Synthetic Microbiology, Marburg, 2014
    • PhD in Biochemistry
      Philipps-University Marburg, Marburg, 2013
    • Diplom (BS/MS) in Chemistry
      Philipps-University Marburg, Marburg, 2010
    Recent Publications See All Publications
    • Journal Article
      The Structural Diversity of Encapsulin Protein Shells.
      Giessen TW. Chembiochem, 2024 Sep 27; e202400535 DOI:10.1002/cbic.202400535
      PMID: 39330624
    • Journal Article
      Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance
      Kwon S, Andreas M, Giessen T. ACS Nano, 2024 Sep 3; DOI:10.1021/acsnano.4c08186
    • Journal Article
      Structural and biochemical characterization of an encapsulin-associated rhodanese from Acinetobacter baumannii.
      Benisch R, Giessen TW. Protein Sci, 2024 Aug; 33 (8): e5129 DOI:10.1002/pro.5129
      PMID: 39073218
    • Journal Article
      Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.
      Szyszka TN, Andreas MP, Lie F, Miller LM, Adamson LSR, Fatehi F, Twarock R, Draper BE, Jarrold MF, Giessen TW, Lau YH. Proc Natl Acad Sci U S A, 2024 May 14; 121 (20): e2321260121 DOI:10.1073/pnas.2321260121
      PMID: 38722807
    • Journal Article
      Cyclodipeptide oxidase is an enzyme filament.
      Andreas MP, Giessen TW. Nat Commun, 2024 Apr 27; 15 (1): 3574 DOI:10.1038/s41467-024-48030-9
      PMID: 38678027
    • Journal Article
      A two-component quasi-icosahedral protein nanocompartment with variable shell composition and irregular tiling.
      Dutcher CA, Andreas MP, Giessen TW. bioRxiv, 2024 Apr 26; DOI:10.1101/2024.04.25.591138
      PMID: 38712103
    • Journal Article
      The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell
      Andreas M, Giessen TW. bioRxiv, 2024 Apr 23;
    • Journal Article
      The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell
      Andreas M, Giessen TW. bioRxiv, 2024 Apr 23;
    Featured News & Stories headshot of Cassandra Dutcher
    Department News
    Congratulations to Cassandra Dutcher, PhD
    Biological Chemistry PhD student Cassandra Dutcher of the Giessen lab at U-M Medical School defends her doctoral dissertation.
    Structure of the filamentous protein cyclodipeptide oxidase AlbAB
    Department News
    The Giessen lab publishes two new papers and receives research awards from the National Science Foundation
    Recent research achievements from the Giessen lab.
    Cutaway view of an self-assembling protein nanocompartment
    Department News
    The Giessen lab publishes a research article in Nature Communications
    The Giessen lab publishes a research article in Nature Communications.