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. Fields of science natural sciencesbiological sciencesbiochemistrybiomoleculesproteinsprotein folding Programme(s) FP4-TMR - Specific research and technological development programme in the field of the training and mobility of researchers, 1994-1998 Topic(s) 0302 - Post-doctoral research training grants TL02 - Molecular Biology and Biochemistry Call for proposal Data not available Funding Scheme RGI - Research grants (individual fellowships) Coordinator University of Cambridge Address Lensfield road CB2 1EW Cambridge GB See on map EU contribution € 0,00 Participants (1) Sort alphabetically Sort by EU Contribution Expand all Collapse all Not available Spain EU contribution € 0,00 Address See on map
