【摘要】 对牛血清白蛋白BSA与阴离子表面活性剂SDS在水溶液中不同浓度和不同相互作用时间的红外光谱进行了研究。研究表明,短时间和低浓度时SDS使BSA的α-螺旋结构增加,无规结构降低,没有破坏蛋白质的二级结构;当SDS浓度很大或者SDS与BSA的作用时间长时,蛋白质的二级结构遭到破坏,BSA的α-螺旋结构降低,无规结构增加。更多还原

【Abstract】 FTIR spectroscopy was applied to investigate the interaction of anionic surfactant Sodium Dodecyl Sulfate (SDS) and Bovine Serum Albumin (BSA). Amide band Ⅰ of BSA was analyzed to obtain the change in secondary structure of BSA when different concentration of SDS was added and during different interaction period. In short interaction period and at low concentration of SDS, the α-helixes increased and the random coil decreased. In long interaction period or at high concentration of SDS, SDS unfolded the protein by decreasing the α-helix structure and increasing the random coil.更多还原