Non-equilibrium conformational dynamics in the function of molecular chaperones

Why do chaperones need ATP hydrolysis to help proteins reach their native, functional states? In this review, we highlight the most recent experimental and theoretical evidences suggesting that ATP hydrolysis allows molecular chaperones to escape the bounds imposed by equilibrium thermodynamics. We argue here that energy consumption must be fully taken into account to understand the mechanism of these intrinsically non-equilibrium machines and we propose a novel perspective in the way the relation between function and ATP hydrolysis is viewed.


Published in:
Current Opinion in Structural Biology, 30, 161-169
Year:
2015
Publisher:
London, Elsevier
ISSN:
0959-440X
Laboratories:




 Record created 2015-04-02, last modified 2018-09-13


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)