CONVERSION OF A LEUCINE ZIPPER INTO A MEMBRANE P

将亮氨酸拉链转变为膜 P

• 批准号: 2020928
• 负责人: CHONGWOO A KIM
• 金额: $ 2.44万
• 依托单位: UNIVERSITY OF CALIFORNIA LOS ANGELES
• 依托单位国家: 美国
• 财政年份: 1996
• 资助国家: 美国
• 起止时间: 1996-11-27 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/2020928
• 关键词: membrane proteins; protein folding; protein sequence

Membrane proteins play crucial roles in many biological processes. Yet, for such an important family of proteins, little is known about their structural properties. If we are to understand the forces which determine folding and assembly leading to proper function of membrane proteins, it is essential to be able to perform experiments on a model system whose structure is known and the effects of mutagenesis can be easily assessed. Of the membrane proteins of known structure, none possess properties which make for an ideal model system: they are either too big making it difficult to assess the effects of mutagenesis or there exist few if any assays to determine proper folding and function of the protein and its mutants. I propose to convert a soluble protein of known structure, the leucine zipper region of GCN4, into a transmembrane protein. Rather than applying a rational de novo design, a genetic approach will be used to select out possible candidate peptides from a pool of sequences. While I hope to learn much from the process of designing such a protein, the eventual goal will be to utilize the converted protein as a model system to study properties of membrane proteins. Ultimately, I hope what is learned from these studies will lead to solving more three dimensional structures of membrane proteins.

膜蛋白在许多生物过程中起着至关重要的作用。然而， 对于如此重要的蛋白质家族，人们对其了解甚少。 结构属性。如果我们要了解 确定折叠和组装，以确保膜的正常功能 蛋白质，能够在模型上进行实验是必不可少的 其结构已知且诱变效果可被 很容易评估。在已知结构的膜蛋白中，没有一个 拥有构成理想模型系统的属性：它们是 太大了，很难评估诱变或那里的影响 几乎不存在任何检测方法来确定正确的折叠和功能 蛋白质及其突变体。我建议将已知的一种可溶蛋白质 结构，GCN4的亮氨酸拉链区域，进入跨膜 蛋白。与其应用理性的从头设计，不如采用基因 将使用一种方法从 序列池。虽然我希望从这个过程中学到很多东西 设计这样一种蛋白质，最终目标将是利用 以转化蛋白为模型体系研究膜的性质 蛋白质。最终，我希望从这些研究中学到的东西将导致 解决更多膜蛋白的三维结构问题。