Cells offer numerous examples of complex protein systems that perform specific tasks with remarkable precision and efficiency. For example, chaperones such as the bacterial GroEL/ES or the eukaryotic TRiC rely on allosteric mechanisms and intricate conformational changes to assist the folding of essential proteins.

We aim to re-engineer these natural systems from scratch using DNA origami, a powerful technique for building complex structures with virtually arbitrary shapes, tuneable dynamics, and switchable conformations. This bottom-up engineering approach will allow us to have full control over structural transitions and allosteric coupling. These artificial systems will not only yield deep insights into protein folding and chaperone functions, but also serve as a stepping stone toward designing nanostructures that carry out novel complex functions.