Chaperonin-encapsulation of proteins for NMR
A novel chaperonin-encapsulation system for NMR measurements has been designed. The single-ring variant SR398 with an ATPase deficient mutation of GroEL, also known as chaperonin, bound co-chaperonin GroES irreversibly, forming a stable cage to encapsulate a target protein. A small GroEL-binding tag made it possible to perform all steps of the encapsulation under near physiological conditions while retaining the native conformation of the target protein. About half of the SR398/GroES cages...[Show more]
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|Source:||Biochimica et Biophysica Acta: Proteins & Proteomics|
|01_Tanaka_Chaperonin-encapsulation_of_2010.pdf||706.87 kB||Adobe PDF||Request a copy|
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