HCS (HPL), HGH AND RELATED PROTEINS

这个项目的长期目标是定义结构-功能 垂体生长激素、促性腺激素释放激素及相关蛋白的关系。 目前的提议试图利用物理化学的差异 HGH和HCS(HPL)之间的关系，目的是理清这些方面 这特别阻止了HCS(HPL)成为强有力的增长促进剂 探员。新的光学技术将被用来搜索天然分子 以获取更多差异。非共价重组体(互补 反应)将被用来准确地确定在 序列位置135和191负责与 前134个残基创造α-螺旋含量和微环境 Trp86和Tyr143，这是每个分子的特征。构象 HGH和HCS(HPL)之间的相似性将与已知 催乳素构象，以确定哪些是负责 这些分子的产乳力几乎相等。同样， 大象生长激素将被分离并研究其构象 进一步确定二级和三级结构特征，这些特征 被所有有效的生长激素高度保守。所有碎片 在这些研究期间产生的，无论是从天然产品中产生的，还是 合成的，将被筛选出抑制任何已知的 人生长激素的生化功能。

The long-term goal of this project is to define the structure-function relationships of pituitary growth hormone, HCS(hPL) and related proteins. The current proposal seeks to exploit the physico-chemical differences between hGH and HCS (hPL) with the intent of sorting out those aspects which specifically prevent HCS (hPL) from being a potent growth promoting agent. New optical techniques will be used to search the native molecules for additional differences. Non-covalent recombinants (complementation reactions) will be employed to establish precisely which residues between sequence positions 135 and 191 are responsible for interacting with the first 134 residues to create the Alpha-helix content and micro-environments of Trp86 and Tyr143, characteristic of each molecule. Conformational similarities between hGH and HCS (hPL) will be correlated with known prolactin conformations in order to establish which are responsible for the nearly equivalent lactogenic potencies of these molecules. Similarly, elephant growth hormone will be isolated and its conformation studied to further identify secondary and tertiary structural characteristics which are highly conserved by all potent growth hormones. All fragments generated during these studies, whether produced from natural products, or synthesized, will be screened for the ability to inhibit any of the known biochemical functions of hGH.