Temperature- and concentration-dependence of compatibility of the organic osmolyte β-dimethylsulfoniopropionate

摘要: Abstract The effects of the organic osmolyte β-dimethylsulfoniopropionate (DMSP) on structural stability three model proteins were examined to determine whether DMSP, like structurally similar solute dimethyl sulfoxide (DMSO), is compatible with native protein structure at low, but not elevated, temperatures. DMSP stabilized phosphofructokinase under conditions cold-induced denaturation. Thus, DMSO, may be an effective cryoprotectant. However, was stabilizer heat Whereas low (0.2 M ) concentrations lactate dehydrogenase against inactivation 50 °C, higher ineffective. favored denaturation glutamate all tested. a osmotic only moderate temperature and yet physiological, concentrations. mechanistic basis DMSP's temperature- concentration-dependent possible roles played by adaptation severity stress in evolutionary selection osmolytes are discussed.