Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins.
It is demonstrated experimentally that addition of proteins that are themselves resistant to denaturation by heat or ethanol can nonspecifically stabilize other proteins that are ordinarily highly susceptible to inactivation. It is proposed that the diffusion-limited rate with which unfolded protein molecules encounter each other and become irreversibly crosslinked is reduced in the presence of substantial concentrations of an unreactive globular protein. We suggest that one of the functions of heat shock proteins, which are synthesized in large amounts after exposure of cells to increased temperature and other forms of stress, may be to stabilize other proteins kinetically in a similarly nonspecific fashion.
D000469:Alkaline Phosphatase; D004220:Disulfides; D000431:Ethanol; D006360:Heat-Shock Proteins; D006358:Hot Temperature; D046911:Macromolecular Substances; D011489:Protein Denaturation; D011506:Proteins / Q000502:physiology*; D012710:Serum Albumin, Bovine; D013917:Thrombin
D004220:Disulfides; D006360:Heat-Shock Proteins; D046911:Macromolecular Substances; D011506:Proteins; D012710:Serum Albumin, Bovine; D000431:Ethanol; D000469:Alkaline Phosphatase; D013917:Thrombin