Total for the last 12 months
number of access : ?
number of downloads : ?
ID 118276
Author
Kawagoe, Soichiro Hokkaido University|Tokushima University
Ishimori, Koichiro Hokkaido University
Keywords
molecular chaperone
biophysical method
multidomain protein
binding kinetics
protein structure
Content Type
Journal Article
Description
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.
Journal Title
International Journal of Molecular Sciences
ISSN
14220067
Publisher
MDPI
Volume
23
Issue
5
Start Page
2485
Published Date
2022-02-24
Rights
© 2022 by the authors. Licensee MDPI, Basel, Switzerland. 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
DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Publisher
departments
Institute of Advanced Medical Sciences