| Abstract: | Molecular chaperones are highly versatile molecules assisting a large variety of folding events during the entire life span of proteins. Chaperones control the folding of proteins into their native structure, repair misfolded proteins and are able to solubilize aggregated proteins. The current knowledge about the functions and molecular mechanisms of chaperones offer new prospects for the biotechnological production of heterologous proteins. Production of high amounts of recombinant proteins results very often in insoluble and inactive proteins. Using molecular chaperones may help to produce high amounts of native and functional protein both in vivo and in vitro. |
