Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding

Kawagoe, Soichiro; Ishimori, Koichiro; Saio, Tomohide

doi:10.3390/ijms23052485

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Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding

by

Soichiro Kawagoe

^1,2

,

Koichiro Ishimori

^1,3,*

and

Tomohide Saio

^2,4,5,*

¹

Graduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-8628, Hokkaido, Japan

²

Graduate School of Medical Sciences, Tokushima University, Tokushima 770-8503, Tokushima, Japan

³

Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 011-0021, Hokkaido, Japan

⁴

Division of Molecular Life Science, Institute of Advanced Medical Sciences, Tokushima University, Tokushima 770-8503, Tokushima, Japan

⁵

Fujii Memorial Institute of Medical Sciences, Institute of Advanced Medical Sciences, Tokushima University, Tokushima 770-8503, Tokushima, Japan

^*

Authors to whom correspondence should be addressed.

Int. J. Mol. Sci. 2022, 23(5), 2485; https://doi.org/10.3390/ijms23052485

Submission received: 9 February 2022 / Revised: 18 February 2022 / Accepted: 21 February 2022 / Published: 24 February 2022

(This article belongs to the Special Issue Biophysical Characterization and Molecular Engineering of Multidomain Proteins 2.0)

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Abstract

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.

Keywords: molecular chaperone; biophysical method; multidomain protein; binding kinetics; protein structure

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MDPI and ACS Style

Kawagoe, S.; Ishimori, K.; Saio, T. Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding. Int. J. Mol. Sci. 2022, 23, 2485. https://doi.org/10.3390/ijms23052485

AMA Style

Kawagoe S, Ishimori K, Saio T. Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding. International Journal of Molecular Sciences. 2022; 23(5):2485. https://doi.org/10.3390/ijms23052485

Chicago/Turabian Style

Kawagoe, Soichiro, Koichiro Ishimori, and Tomohide Saio. 2022. "Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding" International Journal of Molecular Sciences 23, no. 5: 2485. https://doi.org/10.3390/ijms23052485

APA Style

Kawagoe, S., Ishimori, K., & Saio, T. (2022). Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding. International Journal of Molecular Sciences, 23(5), 2485. https://doi.org/10.3390/ijms23052485

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

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Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding

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