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. Author manuscript; available in PMC: 2020 Oct 20.
Published in final edited form as: J Chem Theory Comput. 2010 Aug 30;6(9):2978–2989. doi: 10.1021/ct100334n

Figure 4.

Figure 4.

Inhibition of Hsp90 chaperone function. Client and cochaperone binding to Hsp90 is inhibited by small molecules 6 and 8. COS7 cells were transfected with wild-type Flag–Hsp90. After incubation, cells were treated with 100 μM of the indicated Hsp90 inhibitor for 1 h. Then, cells were lysed, and proteins were immunoprecipitated (IP) by a Flag antibody-conjugated agarose. Indicated coprecipitating proteins were detected by immunoblotting.