Structural Features of Molecular Chaperones: A Possible Micellar Connection

Molecular chaperones are generally proteins, which assist other unrelated proteins to achieve their correct fate in vivo, be that proper folding, oligomeric assembly, subcellular localization, etc. It is not yet known what features of a protein make it a chaperone. Since both protein and non-protein molecules are now known to function as chaperones, we have compared the structural features of many known chaperones to identify common distinctive feature. Our study reveals that many known chaperones have a micelle type organization as a common feature. Even non-protein chaperones have similar structural features. Other factors such as possession of hydrophobic and hydrophilic domains, flexibility of the structure and solubilising capacity of the protein are also important. Based on these features we predicted that tubulin and a random coil protein, α_s-casein may possess chaperone-like activity. These predictions have been verified by experiments in our laboratory and our results clearly show that both tubulin and casein acts as effective molecular chaperones.