Recent advances in understanding catalysis of protein folding by molecular chaperones

• Published in: FEBS letters Vol. 594; no. 17; pp. 2770 - 2781
• Main Authors: Balchin, David, Hayer‐Hartl, Manajit, Hartl, F. Ulrich
• Format: Journal Article
• Language: English
• Published: England 01.09.2020
• Subjects: catalytic activity; chaperonin; chaperonins; confinement; DnaK; GroEL; Hsp40; Hsp60; Hsp70; hydrophobicity; molecular chaperones; protein folding; protein misfolding; Hsp70; Hsp60; DnaK; confinement; GroEL; chaperonin; protein misfolding; protein folding; molecular chaperones; Hsp40

Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress‐induced unfolding. A fundamental function of molecular ch...