Skip to main content
Thomas A Bobik

Thomas A Bobik

  • Professor
  • Biochemistry, Biophysics, and Molecular Biology
Research interests: A main focus of Dr. Bobik's research is bacterial microcompartments (MCPs). Bacterial MCPs are a widespread family of proteinaceous organelles that have diverse roles in bacterial physiology as well as a number of potential biotechnology applications. However, many aspects of MCP structure and function are unknown and only a few types of MCPs have been characterized in any detail. Hence, more research is needed to understand the importance of MCPs among diverse bacteria and to develop MCP-based biotechnologies.

Areas of expertise: Bacterial genetics and metabolism are the main area of expertise in Dr. Bobik's lab. These areas have broad application in biotechnology and biomedicine. The lab's research approach is interdisciplinary involving bacterial genetics, protein biochemistry, biophysics and structural biology

Contact Info

2152 Molecular Bio
2437 Pammel Dr.
Social Media and Websites


  • Post-Doctoral Fellow, Univ. of Utah, Salt Lake City, 1990-95.
  • PhD, Microbiology, Univ. of IL, Urbana, 1990
  • M.S., Microbiology, Univ. of IL, Urbana, 1986
  • B.S., Microbiology, Indiana Univ. Bloomington, IN, 1979

More Information

More background on bacterial microcompartments.

Bacterial Microcompartment
Bacterial MCPs consist of metabolic enzymes encapsulated within a protein shell. This arrangement accelerates catalysis and confines toxic metabolic intermediates. Important research questions include, how are MCPs assembled from thousands of protein subunits and how does a protein shell mediate selective molecular transport.

Bacterial MCPs have broad importance in bacteria.  Bacterial MCPs are distributed among hundreds of species of bacteria, including many pathogens where they perform diverse metabolic functions. However, only a few types of MCPs have been studied in any detail. Hence, more work is needed to appreciate their roles in diverse bacteria and in microbial ecology.


Bacterial MCPs are structurally unique. MCPs are built from thousands of protein subunits and are one of the largest known multi-protein complexes. Unlike other organelles, they consist of metabolic enzymes encapsulated within a protein shell and lack any membrane. This unique design raises varied questions about how they are assembled and the principles that underlie the use of a protein shell for selective molecular transport. Thus, further research on MCPs may reveal new biochemical paradigms some of which might broadly apply to different types of proteins sheets including viral capids and the protein layers that surround a wide variety of cell types.


Bacterial MCPs have several potential applications in biotechnology. The biological function of MCPs is to enhance metabolic processes by accelerating catalysis and confining toxic metabolic intermediates. Hence, they provide a natural starting point for engineering nanobioreactors for the increased production of renewable chemicals and pharmaceuticals.


Bacterial MCPs have a number of associations to human health: With regard to human health, MCPs are linked to enteric pathogenesis and have potential use as drug delivery vehicles. In addition, certain types of MCPs that are prevalent in the human gut microbiome mediate metabolic processes associated with heart disease.