Chaperone-guided protein folding at the single-molecule level

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• Prof. Sander Tans, Delft University of Technology, The Netherlands
• Friday 06 June 2014, 12:00-13:00
• Unilever Lecture Theatre, Department of Chemistry.

If you have a question about this talk, please contact Dr. Judith B. Rommel.

Chaperones have been speculated to affect the protein conformational search for their native state. We address this issue by manipulating single protein chains using optical tweezers. We found that the chaperone Trigger Factor binds folded structures smaller than one domain, which are then stable for seconds and ultimately convert to the native state. Trigger Factor stimulates native folding by suppressing misfolding interactions between domains in constructs of repeated MBP domains. The results indicate that Trigger Factor promotes correct folding by protecting partially folded states from interactions that produce stable misfolded states. As Trigger Factor interacts with most newly-synthesized proteins in Escherichia coli, these findings may be of general importance in understanding protein folding pathways.

This talk is part of the Extra Theoretical Chemistry Seminars series.

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