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Significance Cryo-electron microscopy now shows what many massive protein molecular machines look like. What is needed is a methodology that can probe into the machinery under working conditions. This work demonstrates the ability of hydrogen exchange mass spectrometry to provide detailed structural, biophysical, and functional information on the hexameric 0.6-MDa AAA+ Hsp104 protein in its various static nucleotide-bound states and during functional cycling at near amino acid resolution.

Structural and kinetic basis for the regulation and potentiation of Hsp104 function