Structural studies of bacterial pore-forming protein toxins

这项工作的总体目标是利用X射线结晶学研究重要目标蛋白的三维结构。蛋白质结晶学是研究蛋白质在近原子分辨率下的三维形状的学科。在这种方法中，蛋白质被制成晶体。然后，X射线束照射到晶体上，导致X射线以蛋白质三维形状的特征模式散射。了解蛋白质的结构对于全面了解它们的生物活性是必要的，对于合理设计可能改变它们活性的新药也是非常有用的。大约三分之一的人体蛋白质附着在细胞膜上。然而，人们对这类重要蛋白质的三维结构知之甚少。在这个项目中，正在确定在膜细胞壁中形成孔的蛋白质的结构。这些蛋白质是细菌毒素，对其结构的了解可能会对设计新的抗生素有用。

The general aim of this work is to investigate the three-dimensional structures of important target proteins using X-ray crystallography. Protein crystallography is the study of the three-dimensional shapes of proteins at near atomic resolution. In this method proteins are made to form crystals. X-ray beams are then shone on the crystals causing the X-rays to scatter in a pattern which is characteristic of the protein's three-dimensional shape. Knowledge of the structure of proteins is necessary for the complete understanding of their biological activity and is also very useful for the rational design of new drugs that may alter their activity. Approximately, one third of the body's proteins are attached to membranes. However, relatively little is known about the three-dimensional structures of this important class of proteins. In this project the structures of proteins that form pores in membrane cell walls are being determined. Thses proteins are bacterial toxins and knowledge of their structure may prove useful in the design of new antibiotics.