It is now well accepted that misfolded proteins are severely detrimental to the cell. Evidence for this can be found within every cell from E. Coli to dolphins - in the absolutely vital machinery of the molecular chaperones. Molecular chaperones constitute a natural defence against misfolded proteins. Chaperones can bind and sequester misfolded proteins, stretch them apart to provide a new chance for productive folding or present the misfolded protein to the degradation machinery. We are working extensively with molecular chaperones such as the ER chaperone BiP and the bacterial chaperonin GroEL to understand the function of chaperone recognition of misfolded proteins. Central to this function is protein plasticity – which is a hallmark for both the promiscuity and the specificity for molecular chaperones in binding partially folded substrate proteins. Structural plasticity of proteins is essential for protein-protein interaction, ligand recognition and enzyme activity. The coupling between structural plasticity and biological function is at the core of protein folding, aggregation and interactions with molecular chaperones.
Figure: Chaperone GroEL
Last updated: 2010-02-08