Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

Paolo De Los Rios; Pierre Goloubinoff

doi:10.1038/nsmb.3283

Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

Paolo De Los Rios, Pierre Goloubinoff

Swiss Federal Institute of Technology Lausanne

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

Forceful unfolding by entropic pulling is the general mechanism by which Hsp70 and Hsp110 chaperones control the oligomeric states, structures and activities of cellular proteins.

Original language	English
Pages (from-to)	766-769
Number of pages	4
Journal	Nature Structural and Molecular Biology
Volume	23
Issue number	9
DOIs	https://doi.org/10.1038/nsmb.3283
State	Published - 1 Sep 2016
Externally published	Yes

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abstract = "Forceful unfolding by entropic pulling is the general mechanism by which Hsp70 and Hsp110 chaperones control the oligomeric states, structures and activities of cellular proteins.",

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Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

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