DETERMINATION OF SOLUTION STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN

朊病毒在人类和动物中引起神经退行性疾病。 感染性朊病毒主要由宿主编码的 PrP-Sc的有限消化 蛋白酶K产生N末端截短的多肽 主要对应于残基90- 231，其保持感染性 当注射到正常健康动物体内时。 我们正在研究 重组叙利亚人朊蛋白rPrP（90-231）结构 使用多维核磁共振。 我们使用核磁共振光谱分析， 数据库管理程序（SPARKY）分配骨干网， 蛋白质的侧链1H、13 C和15 N共振。 转让 3000多个NOE的数据管理和约1000个NOE的数据管理 质子共振也使用SPARKY产生。 结构中 细化过程中，我们不断使用分子图形（MidasPlus） 检查我们的计算结果，并显示NMR 约束与程序noeshow。 的互动过程 检查结构和添加约束在很大程度上依赖于 因为我们有很多光谱重叠。 最后，我们使用MidasPlus的分子图形功能， 为出版物和演示文稿制作数字。

Prions cause neurodegenerative diseases in humans and animals. The infectious prions are largely composed of a host encoded glycoprotein denoted PrP-Sc. Limited digestion of PrP-Sc by proteinase K yields an N- terminally truncated polypeptide corresponding primarily to residues 90- 231, which remains infectious when injected into normal healthy animal. We are studying the structure of recombinant Syrian Hamster Prion Protein rPrP(90-231) using multi-dimensional NMR. We use the NMR spectral analysis and database management program (SPARKY) to assign the backbone and sidechain 1H, 13C and 15N resonances of the protein. The assignment for over 3000 NOEs and the management of the data for about 1000 proton resonances are also made using SPARKY. In the structure refinement process, we constantly use molecular graphics (MidasPlus) to check the results of our calculations, and display the NMR constraints with the program noeshow. The interactive process of examining the structure and adding in restraints is heavily dependent on graphics since we have such a great deal of spectral overlap. Finally we use the molecular graphics capabilities of MidasPlus to produce figures for publications and presentations.