The protein folding challenge in psychrophiles: facts and current issues

摘要: Summary The protein folding process in psychrophiles is impaired by low temperature, which exerts several physicochemical constraints, such as a decrease the rate, reduced molecular diffusion rates and increased solvent viscosity, interfere with conformational sampling. Furthermore, assistance required at various steps according to size. Recent studies field have provided contrasting sometimes contradictory results, although generally appears rate-limiting step for growth of psychrophiles. It proposed here that these discrepancies reflect diverse adaptive strategies adopted order allow efficient temperature. Cold adaptations apparently superimpose on pre-existing cellular organization, resulting different strategies. In addition, microbial lifestyle further modulates properties chaperone machinery, possibly explains occurrence cold-adapted non-cold-adapted chaperones