Proteins fold into their functional three-dimensional structure based on the information encoded in the residue sequence 1. In all domains of life, various strategies evolved to assist folding ...

Molecular chaperones act on non-native proteins in the cell to prevent their aggregation, premature folding or misfolding. Different chaperones often exert distinct effects, such as acceleration or ...

When proteins are exposed to stresses like a heat shock, they lose their native structure and form toxic insoluble aggregations. Bacterial molecular chaperone ClpB and its yeast homologue Hsp104 have ...

Proteins are the molecular building blocks and machinery of cells and involved in practically all biological processes. To fulfill their tasks, they need to be folded into a complicated ...

It’s long been known that the proteins that package DNA—like students at a high school dance—require a chaperone. But what exactly that guardian looks and acts like has been a mystery—until now. A ...

Researchers have identified the specific structural loops in G-quadruplex DNA that allow it to act as a chaperone, preventing ...

The 70-kDa heat shock protein (HSP70) family of molecular chaperones represents one of the most ubiquitous classes of chaperones and is highly conserved in all organisms. Members of the HSP70 family ...