DETERMINANTS OF A SIMPLE MEMBRANE PROTIN TOPOLOGY

这项研究旨在更好地了解 膜蛋白获得它们的最终结构。 实验将 检查四个序列元件在建立膜中的作用 E.大肠杆菌丝氨酸化学感受器。 四个序列元素 是蛋白质的两个跨膜片段（tm 1和tm 2），赖氨酸 与tm 2的C-末端相邻的残基（赖氨酸-215），和13 位于tm 2的C-末端8-20个残基的两亲性序列。 提出的实验将识别和分析拓扑 改变不同序列元件的突变的后果。 这些 研究将有助于确定元素的主要顺序要求 功能，并将区分模型如何运作。 另外的实验将研究不同的 序列元件在产生丝氨酸 化学感受器拓扑学

The research proposed aims to provide a better understanding of how membrane proteins acquire their final structures. The experiments will examine the roles of four sequence elements in establishing the membrane topology of the E. coli serine chemoreceptor. The four sequence elements are the protein's two membrane-spanning segments (tm1 and tm2), a lysine residue adjacent to the C-terminal end of tm2 (lysine-215), and a 13 residue amphipathic sequence situated 8-20 residues C-terminal to tm2. The proposed experiments will identify and analyze the topological consequences of mutations altering the different sequence elements. These studies will help define the primary sequence requirements for the elements to function, and will distinguish between models for how they function. Additional experiments will investigate the manner in which the different sequence elements interact with each other in generating the serine chemoreceptor topology.