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主要报导TEM-1β-内酰胺酶的天然蛋白类抑制剂BLIP中一段多肽B1的溶液构象研究结果.在磷酸盐缓冲溶液中，通过圆二色光谱、傅立叶红外光谱和核磁共振谱研究了B1的二级结构特征.实验结果表明，B1在溶液中形成了β-转角结构，为在溶液中单独研究β-转角结构形成与稳定性提供了良好的模板.β-转角在溶液中可以独立存在，表明β-转角在蛋白质折叠过程中可能具有重要作用.
The conformational results of the solution conformation of a polypeptide B1 of BLIP, a natural protein inhibitor of TEM-1β-lactamase, were reported in this paper. In a phosphate buffer solution, the structure of B1 was studied by circular dichroism spectroscopy, Fourier transform infrared spectroscopy and nuclear magnetic resonance spectroscopy Secondary structure.The experimental results show that B1 forms a β-turn structure in solution and provides a good template for studying the formation and stability of β-turn structure in solution.β-turn angle can exist independently in solution, This suggests that β-turn may play an important role in protein folding.