Dr. Brian C. Tripp
Assistant Professor and HTS Coordinator

E-mail: brian.tripp@wmich.edu

Office: 3435 Wood Hall
Lab: 4007 Haenicke Hall

Office Phone: 269 387- 4166

Research Interests

I am primarily a protein biochemist with interests in many areas of protein function, including enzyme catalytic mechanisms and inhibition and association of globular proteins into higher order structures. I also have experience in colloid and surface science. Students in my lab learn a variety of skills including molecular biology, microbiology, liquid chromatography, protein chemistry, UV-visible and fluorescence spectroscopy and high throughput screening approaches. My research interests are currently focused on three distinct areas:

  • Investigating interdisciplinary biotechnology and nanomaterials concepts involving structure-function studies and protein engineering of self-assembling bacterial flagellin proteins, using Salmonella typhimurium flagellin and E. coli FliTrx flagellin expression systems.
  • Investigating fundamental structure-function relationships of mammalian alpha-class isozymes and bacterial gamma-class carbonic anhydrase enzymes and structure-activity relationships of potential small molecule inhibitors of these enzymes.
  • Investigating influence of line tension on mechanism of pore formation and transport in lipid bilayers of cell membranes using biophysical techniques including pendant drop dynamic surface tension, laser tweezers.


The ribbon structure of the Salmonella bacterial flagellin protein. This protein self-assembles by non-covalent interactions into helical flagella fibers composed of up to 30,000 monomers, with assistance provided by the FliD chaperonin protein complex bound on the end of the fibers. These flagella fibers are rotated by a membrane-bound rotary motor to provide propulsion for many types of bacteria. The middle region of this protein sequence varies greatly between species while the ends are highly conserved. The ribbon structure of the archaeal gamma-class carbonic anhydrase (Cam). This is a trimeric enzyme that may use iron instead of zinc, and has structural analogs in other microorganisms, including E. coli. The ribbon structure of the alpha-class mammalian carbonic anhydrase II (CA II). This is a monomeric zinc enzyme with one of the fastest catalytic rates known. At least 14 isozymes of this enzyme are known in mammals; some of which are the targets of some sulfonamide drugs in the treatment of glaucoma and high altitude sickness and some types of cancer.