June 21,10:00am, 2012. Holl 202 in Lu-Jiaxi Building.
Seminar Title: Mechanism of Molecular Chaperone GroEL/GroES in Protein Folding.
Assoc. Prof. Lingling Chen (Indiana University, USA)

Mechanism of Molecular Chaperone GroEL/GroES in Protein Folding

Lingling Chen

Associate Professor

Department of Molecular and Cellular Biochemistry

Indiana University, USA 

Abstract 

Protein folding, a fundamental cellular process, is implicated in human health, and is mediated by molecular chaperones.  GroEL of E. coli along with co-chaperone GroES use an ATP mechanism to assist folding of various proteins in cells.  Mechanism of the GroE system in assisting protein folding has been under both intensive investigations and extensive research efforts.  I will focus on the intriguing properties of substrate protein promiscuity of GroEL and the function of the GroEL-GroES cavity for substrate folding.  I will discuss our unique approaches for structural and biochemical studies of GroEL-substrate protein interaction and the turnover of the GroEL-GroES folding cavity in protein folding.  In addition, I will mention our ongoing structural studies of transcriptional regulation on quorum sensing, a form of bacterial signal transduction.

Dr. Chen obtained her B.S. in Chemistry from Xiamen University in 1988, and continued graduate study in Catalysis.  She went to Stanford University for Ph.D. study in Chemistry, followed by postdoctoral training in protein crystallography at Yale University.  After moving to Indiana University as an independent investigator in 2001, she has focused on mechanistic investigations on molecular chaperone-assisted protein folding and signal transduction via quorum sensing.