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

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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.