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en: Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding.

en: 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.

en: International Journal of Molecular Sciences


en: Regulation of Liquid-Liquid Phase Separation by Molecular Chaperones

ja: 分子シャペロンによる液–液相分離制御

en: Thermal Medicine

ja: Thermal Medicine