Sixteen molecules inhibit hydrolysis of ATP by Hsp104.

<p>Hsp104 (0.25 µM monomer) was incubated for 60 min with ATP (1 mM) plus 16,850 small-molecule drugs (10 µM). The amount of P_i produced was measured by absorbance at 635 nm. Absorbance values were normalized to the absorbance produced by Hsp104 in the absence of the small molecules. Sixteen molecules were found to reproducibly interfere with Hsp104 ATPase activity. Inhibition values represent mean ±S.D. (<i>n</i> = 2).</p><p>Sixteen molecules inhibit hydrolysis of ATP by Hsp104.