|Title:||Chaperonin-encapsulation of proteins for NMR.|
Dixon, Nicholas E
Matsuzaki, Katsumi https://orcid.org/0000-0002-0182-1690 (unconfirmed)
Hoshino, Masaru https://orcid.org/0000-0003-4099-0232 (unconfirmed)
|Author's alias:||星野, 大|
|Journal title:||Biochimica et biophysica acta|
|Abstract:||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.|
|Rights:||© 2010 Elsevier B.V.|
This is not the published version. Please cite only the published version.
|Appears in Collections:||Journal Articles|
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