Zhaohui Xu focuses on the in vivo process of protein folding and protein translocation.

Since all proteins need to be folded into a defined structure and transported to a particular location to be fully functional, protein folding and translocation are vitally important for the health and survival of cells. Failures in these processes have been directly linked to many human diseases. While his lab has a strong emphasis on structural biology, they also combine biochemistry, biophysics and genetics to pursue their mechanistic and functional studies.

A group of proteins call molecular chaperones are of particular interest to Dr. Xu. These proteins function to ensure that other proteins will fold correctly into their native structures. For years, the concept of molecular chaperones was foreign to many people and it was not clear how it might work. During his postdoctoral work, Dr. Xu determined the structure of one of the most interesting molecular chaperones called GroEL, in complex with its co-chaperone GroES. The structure was considered as a landmark in the field as it clearly reveals the molecular mechanism regarding the function of GroEL.

Office: Room 3163B
Life Sciences Institute
Mary Sue Coleman Hall
210 Washtenaw Avenue
Ann Arbor, MI 48109-2216

Research Areas

  • protein folding
  • molecular chaperones
  • structural biology
  • membrane trafficking
  • B.S.,Biology, University of Science and Technology of China (1989)
  • Ph.D., Biochemistry, University of Minnesota (1992)
  • Postdoctoral training, Howard Hughes Medical Institute, Yale University (1993–1998)
  • Biological Scholar, U-M Medical School (1999)
  • Pew Scholar in the Biomedical Sciences (2001)
  • Basic Science Research Award, U-M Medical School (2003)