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Chaperoning single proteins

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Various chaperones are known to bind exposed protein-chains, and hence protect them from aggregation before folding starts, and to rescue them when they are misfolded. Using optical tweezers, we explore how chaperones affect the folding of single proteins. We show that various chaperones interact with folded protein structures, and hence actively help solve their conformational search for the native state. They exploit diverse mechanisms, ranging from stimulating local folding to ATP -driven capture and release of partially folded protein structures. The results indicate that chaperones perform more intricate tasks than previously assumed, and bring a new perspective to the protein-folding problem

This talk is part of the Biophysical Seminars series.

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