Research: Project 1
Chaperone-assisted membrane protein folding
YidC/Oxa1/Alb3 is a membrane protein family that plays a critical role in folding and assembly of membrane proteins in the inner membranes of bacteria, mitochondria, and chloroplasts. In E. coli, YidC forms a membrane insertion pore independent of SecYEG complex, major protein translocation machinery. YidC also has a chaperone activity: it facilitates the folding of a variety of SecYEG-dependent proteins. To understand how YidC acts as chaperone, we will tackle three specific problems.
- What are the driving forces in YidC-substrate interaction?
- How does YidC facilitate folding of membrane proteins?
- How are the structure and dynamics of YidC related to the function?