During their formation within the cells, many proteins rely on the assistance of molecular protectors, so-called chaperones. They help the proteins to fold correctly and thus ensure the right final structure. The roles of chaperones in membrane protein folding have long remained unclear. Researchers at the Biozentrum, University of Basel, and at ETH Zurich have now shown how chaperones stabilize an immature bacterial membrane protein and guide it in the right folding direction, thus protecting it from misfolding. Their study was recently published in Nature Structural & Molecular Biology.
Chaperones (light blue) promote the insertion and folding of the bacterial membrane protein FhuA (yellow).
Image credit:University of Basel, Biozentrum