直近一年間の累計
アクセス数 : ?
ダウンロード数 : ?
ID 117462
著者
Kawagoe, Soichiro Hokkaido University|Tokushima University
Ishimori, Koichiro Hokkaido University
キーワード
molecular chaperone
biophysical method
multidomain protein
binding kinetics
protein structure
資料タイプ
学術雑誌論文
抄録
Despite recent developments in protein structure prediction, the process of the structure formation, folding, remains poorly understood. Notably, folding of multidomain proteins, which involves multiple steps of segmental folding, is one of the biggest questions in protein science. Multidomain protein folding often requires the assistance of molecular chaperones. Molecular chaperones promote or delay the folding of the client protein, but the detailed mechanisms are still unclear. This review summarizes the findings of biophysical and structural studies on the mechanism of multidomain protein folding mediated by molecular chaperones and explains how molecular chaperones recognize the client proteins and alter their folding properties. Furthermore, we introduce several recent studies that describe the concept of kinetics–activity relationships to explain the mechanism of functional diversity of molecular chaperones.
掲載誌名
International Journal of Molecular Sciences
ISSN
14220067
出版者
MDPI
23
5
開始ページ
2485
発行日
2022-02-24
権利情報
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
EDB ID
出版社版DOI
出版社版URL
フルテキストファイル
言語
eng
著者版フラグ
出版社版
部局
先端酵素学研究所