Molecular Origami

The folding of a protein closely resembles a subtle work of origami, where something can easily go wrong.

That is why all cells, even bacteria, employ so-called chaperones to assist in this folding process. AMOLF researchers, led by Sander Tans, and researchers of the Groningen University have now been able to observe how these chaperones work by getting a hold on the end of a single protein.

It appears that, in a certain way, they take a hold of the protein chain, just after it has been made, so that the chain has to wait a while before it can start folding. The results are important for a better understanding of the folding process of proteins. This is important to gain more knowledge about diseases that originate in the aggregation of proteins, such as Alzheimer's disease. The researchers published their results in the 30 November edition of Science.

Proteins are made in a long chain. They can only play their role in the cell when they are folded. The spontaneous step-by-step folding of the protein closely resembles a subtle work of origami. Therefore, this can easily go wrong. These errors are at the basis of, for example, Alzheimer's disease. When proteins stop folding in their normal patterns, they can start to aggregate and thereby disrupt cell function. To prevent this aggregation, all cells, even bacteria, employ so-called chaperones, which are also proteins. For a better understanding of the folding of proteins, insight into the role of chaperones is essential. That is why intensive research is focused on this field. One of the difficulties the researchers encounter is directly measuring the effect of chaperones on protein folding, since the billions of proteins in one test tube all fold simultaneously.