ARTIFICIAL CHAPERONE FOR RODLIKE PROTEIN STRUCTURE

描述（改编自摘要）：尾部纤维连接到底部的 噬菌体T4是一种天然的化学机械传感器， 在150 nm外的宿主细胞表面上的化学识别信号。博士 Goldberg建议利用尾纤维的独特结构特性， 新型自组装部件重新设计的仿生基础 从分子水平。合理的基因重新设计这些自然的 将组分自组装成蛋白质试剂盒， 结构将需要尾部纤维段的精确模型及其 原子分辨率的关节。研究人员发明了一种方法， 为了克服这个问题， 大的轴比，使NMR分析和晶体形成 很难，如果不是不可能的话。此外，相对低的分子量 将有助于收集有用的NMR谱。整体 目的是解决T4尾纤的总体结构。作为原子模型进行 杆和接头将有助于它们的重新设计， 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.