论文部分内容阅读
β-发夹是天然蛋白质中丰富的二级结构单元之一,在蛋白折叠和功能方面扮演着重要角色.文章报导了二条多肽序列（LTVd-PGLTV,n7和LTVGDDTV,n5）的设计、合成和园二色谱研究结果.结果显示,n5在 198nm附近呈现负峰,表现为非规整结构特征;相反,n7表现为典型的发夹结构特征,在218nm附近呈负峰,196nm附近呈正峰,为β-转角与β-折叠的共同贡献.初步研究表明,β-转角、序列关系和氨基酸形成在折叠结构倾向性是β-发夹结构形成和稳定的决定性因素.
β-hairpin is one of the abundant secondary structural units in natural proteins and plays an important role in protein folding and function.In this paper, we report the design, synthesis and application of two polypeptide sequences (LTVd-PGLTV, n7 and LTVGDDTV, n5) The results showed that n5 showed a negative peak near 198 nm, which was characterized by irregular structure. On the contrary, n7 showed typical hairpin structure with a negative peak around 218 nm and a positive peak around 196 nm - the common contribution of the corners to the β-sheet.Preliminary studies have shown that β-turn, sequence relationships and amino acid formation in the folded structure tendencies are decisive factors in β-hairpin structure formation and stability.