Molecular chaperones molecules

Brodsky JL, Chiosis G (2006) Hsp70 molecular chaperones emerging roles in human disease and identification of small molecule modulators. Curr Top Med Chem 6 1215-1225... 

Wright CM, Chovatiya RJ, Jameson NE et al (2008) Pyrimidinone-peptoid hybrid molecules with distinct effects on molecular chaperone function and cell proliferation. Bioorg Med Chem 16 3291-3301... 

Other larger molecules require the assistance of proteins called molecular chaperones to ensure correct folding. 

One of the most important aspects of protein synthesis is the folding of polypeptides into their biologically active conformations. Despite decades of investigation into the physical and chemical properties of polypeptide chains, the mechanism by which a primary sequence dictates the molecule s final conformation is unresolved. It has become increasingly clear that many proteins require molecular chaperones to fold into their final three-dimensional conformations. Protein mis-folding is now known to be an important feature of several human diseases, including Alzheimer s disease and Creutzfeld-Jacob disease. 

Dymock BW et al (2005) Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J Med Chem 48(13) 4212-4215... 

Vassilakos, A., Cohen-Doyle, M. F., Peterson, P. A., Jackson, M. R., and Williams, D. B. (1996). The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15, 1495-1506. 

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