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 ...

The structure and chaperone function of DmHsp22WT, a small Hsp of Drosophila melanogaster localized within mitochondria were examined. Mutations of conserved arginine mutants within the ...

The first full-length structures of two heat shock chaperone proteins in a complex reveal the key structural region regulating their function, according to a new study from St. Jude Children's ...

Cell Stress & Chaperones publishes basic and applied research on cellular stress responses of animals, microorganisms, and plants. Cell stress is broadly defined to include cellular responses to heat ...

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 ...

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 ...

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 ...

Proteins need to fold into specific shapes to perform their functions in cells, but they occasionally misfold, which can ...