用2D—NMR测定人卵泡促性腺激素释放肽（hF—GRP）的溶液构象

• 作 者: 吴宏伟 林克椿 翟纯
• 机 构: 北京医科大学生物物理系
• 出 处: 生物物理学报
• 发表日期: 1995年03期
• 关键词: 促性腺激素 GRP NMR hF 激素类 无规卷曲 距离信息 化学位移 羧基端 脉冲序列

人卵泡促性腺激素释放肽是１９８７年才被发现的一种激素类１４肽，本文利用２Ｄ—ＮＭＲ技术（ＴＯＣＳＹ，ＲＯＥＳＹ）首先测定了它的溶液构象，在残基归属的基础上，据ＲＯＥＳＹ距离信息得到该１４肽的初步构象为，羧基端三个残基是运动性较大的无规卷曲，氨基端Ｔｈｒｌ的侧链靠近主链，Ｈｉｓ１０－Ｐｒｏｌｌ间的肽链以ｔｒａｎｓ构型占优势，在Ｓｅｒ４—Ｈｉｓ５—Ｈｉｓ６区域可能形成一个部分类似β－转角Ⅱ的弯曲。

Human follicular gonadotrophin-releasing peptide was a hormone peptide discovered only in 1987. In this paper, the solution conformation was first determined by 2D-NMR technique (TOCSY, ROESY). Based on the residue assignment, according to ROESY The initial conformation of the 14-peptide was obtained from the distance information. The three residues at the carboxyl terminal were random coils with greater motility. The side chain of the Thrl at the amino terminal was close to the main chain and the peptide chain between His10-Proll was dominated by the trans configuration , It is possible to form a bend in the Ser4-His5-His6 region that is similar to β-turn II.