STRUCTURAL STUDIES ON T4 LYSOZYME MUTANTS

T4 溶菌酶突变体的结构研究

• 批准号: 6119526
• 负责人: Martin Sagermann
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119526
• 关键词: biomaterials; proteins; structural biology

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.

我们的实验室长期以来一直对 噬菌体T4溶菌酶研究 大多数研究集中在 这种酶的稳定性和折叠特性。 与 建议的实验，我们想调查的住宿 插入到环结构和突变蛋白中， 区域被具有高螺旋形成的序列取代， 倾向 该建议分为三个部分。 在前两项中，只有 中到低分辨率的数据集可以在内部获得， 必须提高衍射数据的质量，以便能够 了解结构变化。 在第三部分中，我们希望使用 同步加速器首次获得1E高分辨率 酶的结构并解决X射线之间的争议 数据和理论计算。