We are interested in structure and function of proteins involved in important biological processes that are related to human diseases or microbial infections. One of our projects is focused on molecular chaperone Hsp60. Hsp60 is essential for cellular viability, and its main function is to mediate folding of cellular proteins. We focus on mechanistic investigations of human mitochondrial mHsp60. Since mHsp60 is associated with various human health conditions, it has been proposed as potent drug targets and biomarkers. To provide structural basis for drug targeting, we study structure and mechanism of mHsp60 using a range of molecular biology, biochemical, and particularly structural methods of X-ray crystallography and cryogenic electron microscopy (cryo EM).


  • Structure, Function and Mechanism of Molecular Chaperone Hsp60

We currently focus on molecular chaperone Hsp60.

One of our projects is to investigate the mechanism of human mitochondrial mHsp60-mHsp10.

Research Interests:

  • Microbial structure, function and mechanism; evolution of chaperonin Hsp60; cryo-EM studies of human mitochondrial Hsp60

Subject Area:

  • Molecular and Cellular Biochemistry.

Research Interests:

  • Microbial structure, function and mechanism; biology of molecular chaperone (chaperonin).
Past Affiliations
Biochemistry, Molecular Biology, Biological Science, Cellular Biochemistry, Molecular Biochemistry
PhD, Stanford University, Chemistry, 1996
BS, Xiamen University, Xiamen, China, Physical Chemistry, 1988