Molecular chaperones are proteins and protein complexes that bind to misfolded or unfolded polypeptide chains and affect the subsequent folding processes of these chains. All proteins are created at the ribosome as straight chains of amino acids, but must be folded into a precise, three-dimensional shape (conformation) in order to perform their specific functions. The misfolded or unfolded polypeptide chains to which chaperones bind are said to be "non-native," meaning that they are not folded into their functional conformation. Chaperones are found in all types of cells and cellular compartments, and have a wide range of binding specificities and functional roles.

Discovery of Chaperones

Chaperones were originally identified in the mid-1980s from studies of protein folding and assembly in plant chloroplasts. A new protein was identified that was required for correct folding of a large enzyme complex in chloroplasts, yet the mysterious protein was not associated with...