The general concept of molecular chaperones

This introductory article proposes a conceptual framework in which to consider the information that is emerging about the proteins called molecular chaperones, and suggests some definitions that may be useful in this new field of biochemistry. Molecular chaperones are currently defined in functional terms as a class of unrelated families of protein that assist the correct non-covalent assembly of other polypeptide-containing structures in vivo, but which are not components of these assembled structures when they are performing their normal biological functions. The term assembly in this definition embraces not only the folding of newly synthesized polypeptides and any association into oligomers that may occur, but also includes any changes in the degree of either folding or association that may take place when proteins carry out their functions, are transported across membranes, or are repaired or destroyed after stresses such as heat shock. Known molecular chaperones do not convey steric information essential for correct assembly, but appear to act by binding to interactive protein surfaces that are transiently exposed during various cellular processes; this binding inhibits incorrect interactions that may otherwise produce non-functional structures. Thus the concept of molecular chaperones does not contradict the principle of protein self-assembly, but qualifies it by suggesting that in vivo self-assembly requires assistance by other protein molecules.