This article has been widely quoted since it was the first review to discuss a new functional class of proteins called molecular chaperones. These proteins function by assisting the assembly/disassembly of other protein-containing structures without forming a part of these structures when the latter are functioning normally. It was work on chloroplast biogenesis in my laboratory the early 1980s that identified the first example of a protein that binds transiently to a newly synthesized polypeptide. This binding enables that polypeptide to avoid aggregation and so allows it to assemble correctly into its functional form. Many more examples of similar functions were then discovered in all types of cells. Prior to this discovery, protein assembly was thought to be a spontaneous process of self-assembly, but the discovery of the chaperone function has replaced that view with the concept of assisted self-assembly. Currently at least 30 different families of proteins have been to shown act as molecular chaperones in a wide variety of biochemical processes.

Emeritus Professor R. John Ellis, FRS
Department of Biological Sciences
University of Warwick
United Kingdom