HCS (HPL), HGH AND RELATED PROTEINS

本项目的长期目标是确定结构-功能 垂体生长激素与HCS（hPL）及其相关蛋白的关系。 目前的建议试图利用物理化学差异 hGH和HCS（hPL）之间的关系，目的是理清这些方面 这专门阻止HCS（hPL）成为有效的生长促进剂 剂 新的光学技术将被用来寻找天然分子 更多的差异。 非共价重组体（互补 反应）将被用来精确地确定哪些残留物之间 序列位置135和191负责与 前134个残基，以创建α-螺旋内容和微环境 Trp 86和Tyr 143，每个分子的特征。 构象 hGH和HCS（hPL）之间的相似性将与已知的 催乳素构象，以确定哪些是负责 这些分子的催乳效力几乎相等。 同样地， 大象生长激素将被分离出来，并对其构象进行研究， 进一步鉴定二级和三级结构特征， 是所有强效生长激素高度保守的。 所有片段 在这些研究中产生的，无论是从天然产品中产生的，还是 将筛选抑制任何已知的 hGH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.