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The conformation of a protein is responsible for its biological activity.The investigation in the folding/unfolding mechanism of proteins,especially the conformational changes in the complex proteins contain multidomain structures,is of great biological importance for the elucidation of the pathogenetic mechanism caused by misfolding and the development of the effective treatment.Moreover,the studies provide a basis for research on how to utilize the special activities caused by the conformational change during the protein unfolding processes in biology,medicine,and chemistry.In this research,electrochemical techniques were used to investigate the conformational change in the complex multidomain protein of bovine serum albumin (BSA) and hemoglobin (Hb),which was used in biology and chemistry through modulating their conformations.