Folding of n-(5'phosphoribosyl - anthranilate isomerase in the presence and absence of groel

Project Information

Grant agreement ID: FMBI950246

Project closed

Start date 10 January 1996

End date 9 January 1998

Funded under

• Specific research and technological development programme in the field of the training and mobility of researchers, 1994-1998

Total cost No data

EU contribution No data

Coordinated by

University of Cambridge
United Kingdom

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 sciences › biological sciences › biochemistry › biomolecules › proteins › protein 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

• EU contribution: No data
• Address: Lensfield Road ; CB2 1EW Cambridge ; United Kingdom
• Total cost: No data

Participants (1)

Not available

Spain

• EU contribution: No data
• Total cost: No data