CONVERSION OF A LEUCINE ZIPPER INTO A MEMBRANE P

膜蛋白在许多生物过程中起着至关重要的作用。 然而， 对于这样一个重要的蛋白质家族，人们对其 结构特性 如果我们要理解 确定折叠和组装，以使膜发挥正常功能 蛋白质，它是必不可少的，能够进行实验的模型 系统的结构是已知的，诱变的效果可以 容易评估。 在已知结构的膜蛋白中， 具有理想模型系统的性质：它们是 太大，难以评估诱变的影响， 存在很少的（如果有的话）测定来确定所述蛋白的正确折叠和功能的测定。 蛋白质及其突变体。 我建议将已知的可溶性蛋白质 结构，GCN 4的亮氨酸拉链区，进入跨膜 蛋白而不是应用一个理性的从头设计，一个遗传 方法将被用来从一个可能的候选肽中选择出可能的候选肽。 序列池。 虽然我希望从这个过程中学到很多东西， 设计这样的蛋白质，最终的目标将是利用 转化蛋白质作为研究膜性质的模型体系 proteins.最终，我希望从这些研究中学到的东西将导致 来解决更多的膜蛋白的三维结构。

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.