STRUCTURAL STUDIES ON T4 LYSOZYME MUTANTS

我们的实验室长期以来一直对结构 噬菌体T4溶菌酶的研究大多数研究都集中在 该酶的稳定性和折叠特性。与 我们想要调查的拟议实验的住宿 插入到环状结构和突变蛋白中的β-折叠 区域被具有高螺旋形成的序列所取代 倾向性。该提案分为三个部分。在前两部中，只有 中低分辨率数据集可以在内部获得，它是 必须提高衍射数据的质量才能 了解结构性变化。在第三部分中，我们希望使用 第一次获得1E高分辨率的同步加速器 解决了酶的结构和X射线之间的争议 数据和理论计算。

Our lab has a long standing interest in the structural investigation of phage T4 lysozyme. Most of the research focuses on the stability and folding characteristics of this enzyme. With the proposed experiments we would like to investigate accommodations of insertions into loop structures and mutant proteins where beta-sheet regions are replaced by sequences that have a high helix forming propensity. The proposal is in three parts. In the first two, only medium to low resolution datasets could be obtained in house and it is necessary to improve the quality of the diffraction data to be able to understand the structural changes. In the third part we wish to use the synchrotron to obtain, for the first time, a 1 E high resolution structure of the enzyme and to resolve a controversy between the X-ray data and theoretical calculations.