Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones
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DOI: 10.3390/biom12060832
Abstract: Recent experimental studies suggest that ATP-driven molecular chaperones can stabilize protein substrates in their native structures out of thermal equilibrium. The mechanism of such nonequilibrium protein folding is an open question. Based on available structural… read more here.
Keywords: protein folding; atp driven; folding activation; driven chaperones ... See more keywords