ID | 118276 |
Author |
Kawagoe, Soichiro
Hokkaido University|Tokushima University
Ishimori, Koichiro
Hokkaido University
Saio, Tomohide
Tokushima University
Tokushima University Educator and Researcher Directory
KAKEN Search Researchers
|
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
|