Access count of this item: 204

Files in This Item:
File Description SizeFormat 
j.bbapap.2009.12.016.pdf266.87 kBAdobe PDFView/Open
Title: Chaperonin-encapsulation of proteins for NMR.
Authors: Tanaka, Shinji
Kawata, Yasushi
Otting, Gottfried
Dixon, Nicholas E
Matsuzaki, Katsumi  kyouindb  KAKEN_id
Hoshino, Masaru  kyouindb  KAKEN_id
Author's alias: 星野, 大
Keywords: Aggregation
GroE
Molecular chaperone
NMR
Protein encapsulation
Issue Date: Apr-2010
Publisher: Elsevier
Journal title: Biochimica et biophysica acta
Volume: 1804
Issue: 4
Start page: 866
End page: 871
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. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
URI: http://hdl.handle.net/2433/108262
DOI(Published Version): 10.1016/j.bbapap.2009.12.016
PubMed ID: 20045085
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks


Export Format: 


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.