Folding of n-(5'phosphoribosyl - anthranilate isomerase in the presence and absence of groel
FP4 — Training and Mobility of Researchers
- Duration
- 1996-01-10 → 1998-01-09
- EU contribution
- —
- Participants
- 2
- Scheme
- RGI
Lines connect the coordinator with its partners. CORDIS does not always give exact coordinates for projects before 2014. These points are placed at city or country level.
Project objective
The Escherichia coli chaperonins GroEL and GroES facilitate protein folding in vivo and in vitro. However, the mechanism of action is not well understood. N-(5'Phosphoribosyl)anthranilate isomerase from E. coli (ePRAI), an alpha/Beta barrel protein, will be used as substrate for the chaperonin. The proposed project will address the following specific aspects of the activity of GroEL: 1) To determine if the chaperonin modifies the folding pathway of ePRAI. 2) To determine the role of ATP and GroES in the folding mechanism. 3) To determine at which stage of the folding pathway and what region of ePRAI interacts with GroEL.
Original text from CORDIS.
Participants
- University of Cambridge · CambridgeCoordinatorUnited Kingdom
- Not availableCity levelSpain
Links
Data: CORDIS, © European Union
