NMR Structure of Membrane Proteins of T. maritima

描述（由申请人提供）：膜蛋白结构测定对于结构生物学家来说是一项艰巨的任务。膜蛋白占蛋白质组的30%。然而，只有约30个独特的结构已被确定，使其对蛋白质数据库的贡献不到0.5%。大多数膜蛋白是跨膜螺旋束，但在已知的结构中，大约一半是β-桶蛋白，其仅限于细菌、线粒体和叶绿体的外膜。本研究的目标螺旋膜蛋白与两个，三个，和四个预测的跨膜段的NMR结构测定，以显着多样化的不同类型的膜蛋白结构已知的。由于错误折叠和功能丧失，在许多疾病中已经鉴定出有缺陷的膜蛋白，使其成为药物设计的靶点。结构信息可以提高这些药物追踪的有效性。此外，更多的螺旋跨膜结构将有助于理解膜蛋白的稳定性，并增加预测膜蛋白结构的可能性。

DESCRIPTION (provided by applicant): Membrane protein structure determination is a difficult task for structural biologists. Membrane proteins comprise 30% of the proteome. However, only ~30 unique structures have been determined, making their contribution to the protein data bank less than 0.5%. The majority of membrane proteins are transmembrane helical bundles, but of the known structures roughly half are beta-barrel proteins, which are limited to the outer membrane of bacteria, mitochondria, and chloroplasts. This study targets helical membrane proteins with two, three, and four predicted transmembrane segments for NMR structure determination in order to significantly diversify the different types of membrane protein structures known. Defective membrane proteins have been identified in many diseases due to misfolding and loss of function making them targets for drug design. Structural information could advance the effectiveness of these drug pursuits. In addition, more helical transmembrane structures will aid in the understanding of membrane protein stability and increase the likelihood of predicting membrane protein structures.