ARTIFICIAL CHAPERONE FOR RODLIKE PROTEIN STRUCTURE

描述(摘自摘要)：附着在底座上的尾部纤维 噬菌体T4是一种天然的化学机械传感器，它可以通过机械反应 到150纳米外的宿主细胞表面的化学识别信号。Dr。 Goldberg建议利用尾部纤维的独特结构特性作为 新型汽车自装配零部件再设计的仿生学基础 来自分子水平的材料。合理的基因重新设计这些天然的 将组分自组装成蛋白质试剂盒，用于自组装有用的 结构将需要尾部纤维段和它们的精确模型 原子分辨率的关节。调查人员已经设计出一种方法来制作 为了克服这个问题，蛋白质棒的小重叠片段 具有很大的轴比，这使得核磁共振分析和晶体形成 困难，如果不是不可能的话。此外，相对较低的分子量 碎片的收集将有助于收集有用的核磁共振谱。整体而言 目标是解决T4尾纤的总体结构。分子的原子模型 杆和接头将有助于它们的重新设计，使其更实用 用于医疗和非医疗用途。

DESCRIPTION (Adapted from abstract): The tail fiber attached to the base of bacteriophage T4 is a natural chemomechanical sensor which reacts mechanically to a chemical recognition signal, on the host cell surface, 150 nm away. Dr. Goldberg proposes to use the unique structural properties of the tail fiber as a biomimetic basis for redesign of the parts for self-assembly of new types of materials from the molecular level. Rational genetic redesign of these natural self-assembling components into protein kits for self-assembly of useful structures will require an accurate model of the tail fiber segments and their joints at atomic resolution. The investigators have devised a method for making small overlapping fragments of the protein rod in order to overcome the problem of a large axial ratio which makes both NMR analysis and crystal formation difficult, if not impossible. In addition, the relatively low molecular weight of the fragments will facilitate collection of useful NMR spectra. The overall goal is to solve the total structure of the T4 tail fiber. The atomic model of the rods and joints will serve to facilitate their redesign for more practical purposes for both medical and non-medical uses.