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Models of the Hsp90 conformational cycle and the impact of appending a dimeric coiled-coil to the N terminus. A, for wild-type Hsp90, ATP binding and hydrolysis lead to large conformational rearrangements. B, our observations with coil-NMC demonstrate that imposing N-domain proximity dramatically decreases the magnitude of these conformational rearrangements, yet remains compatible with function in yeast.
