NMR analysis of amyloid beta-oligomer by using molecular chaperone encapsulation system.

核磁共振波谱是分析溶液中蛋白质结构和动力学的有力工具。然而，该技术无法分析聚集的蛋白质和处于缔合和解离平衡的蛋白质。为了克服这一主要缺点，将目标蛋白封装到由大肠杆菌分子伴侣组成的“笼子”中是有效的。作为分子伴侣封装系统开发的第一步，利用绿色荧光蛋白作为模型底物分析了分子伴侣胶囊的长期稳定性。

Nuclear magnetic resonance spectroscopy is a powerful tool for the analysis of protein structure and dynamics in solution. This technique is, however, not able to analyze aggregated proteins and proteins which is in equilibrium in association and dissociation. To circumvent this major disadvantage, it is effective to encapsulate the target protein into the 'cage' composed of molecular chaperone from Escherichia coli. As a first step of the development of molecular chaperone encapsulating system, the long term stability of the molecular chaperone capsule was analyzed by using a green fluorescence protein as a model substrate.