We are interested in structure and function of proteins involved in important biological processes that are related to human diseases or microbial infections. Our research proteins include those of molecular chaperone, transcription factor, and microbial effector that are important in protein quality control, signal transduction and microbial-host interaction, respectively. To investigate how proteins function at the molecular level, we apply a range of molecular biology, biochemical, and particularly structural methods of X-ray crystallography and cryogenic electron microscopy (Cryo EM).

We currently focus on molecular chaperone Hsp60. Hsp60 is essential for cellular viability, and it is highly conserved among three kingdoms of life. The main function of Hsp60 is, together with its cochaperone Hsp10, to mediate folding of cellular proteins. One of our projects is to investigate the mechanism of human mitochondrial mHsp60-mHsp10. Since mHsp60 is associated with various human health conditions, it has been proposed as possible drug targets and biomarkers. To provide structural basis for mechanistic understanding and drug targeting, we are determining structures of mHsp60-mHsp10 using Cryo EM.