In most cases : a protein that is specialized for folding/stabilization or direction of a (typically newly synthesized) protein. A chaperone may bind to a nascent protein either co-translationally or following translation. Although most chaperones are proteins, a membrane lipid acts as a chaperone for the LacY protein in Escherichia coli.
A continuing challenge for biochemists is to unravel the processes required to convert the one-dimensional information encoded within genes (i.e., an amino acid sequence) into three-dimensional protein structures that contain biochemical activity. Historically, protein biogenesis was thought to involve only spontaneous folding of polypeptide domains.
We now realize that the process is more complex than previously envisioned. Most, if not all, proteins in the living cell require assistance to fold properly. This assistance comes from proteins that are not final components of the assembled product. These “foldases” are called chaperones (or chaperonins, depending on their structure).
The proposed function of chaperone proteins is to assist polypeptides to selfassemble by inhibiting alternative assembling pathways that produce nonfunctional structures. During protein synthesis, for example, the amino-terminal region of each polypeptide is made before the carboxy-terminal region. The chance of incorrect folding of a nascent polypeptide is reduced through interaction with chaperones.
Another process in which chaperones can be invaluable is protein secretion or translocation. Proteins that cross membranes do so in an unfolded or partially folded state. Often they are synthesized by cytosolic ribosomes and must be prevented from folding into a translocation-incompetent state. Cells also take advantage of chaperonins when faced with an environmental stress that will denature proteins into inactive forms that aggregate.
To protect against such stresses, cells accumulate proteins that prevent the production of these aggregates or unscramble the aggregates so that they can correctly reassemble .