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Chaperonin-encapsulation of proteins for NMR
Faculty of Science - Papers (Archive)
  • Shinji Tanaka, Kyoto University
  • Yasushi Kawata, Tottori University
  • Gottfried Otting, Australian National University
  • Nicholas E Dixon, University of Wollongong
  • Katsumi Matsuzaki, Kyoto University
  • Masaru Hoshino, Kyoto University
Publication Date
Publication Details

Matsuzaki, K., Kawata, Y., Hoshino, M., Dixon, N. E., Otting, G. & Tanaka, S. (2010). Chaperonin-encapsulation of proteins for NMR. BBA - Proteins and Proteomics, 1804 (4), 866-871.

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 encapsulated target protein molecules. As binding only depends on the 12-residue tag sequence, this encapsulation method is applicable to a large number of proteins. Isolation of the target proteins in the molecular cage of chaperonin will allow the study of highly aggregation-prone proteins by solution NMR.
Citation Information
Shinji Tanaka, Yasushi Kawata, Gottfried Otting, Nicholas E Dixon, et al.. "Chaperonin-encapsulation of proteins for NMR" (2010)
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