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. Author manuscript; available in PMC: 2013 May 15.
Published in final edited form as: Bioorg Med Chem. 2012 Mar 29;20(10):3298–3305. doi: 10.1016/j.bmc.2012.03.043

Figure 2. Directed chemical evolution of a selective affinity resin for Hsp90.

Figure 2

SDS-PAGE silver stain showing the effects of different side chain modifications on Hsp90 recovery and recovery of non-specifically bound proteins. Selectivity towards Hsp90 was demonstrated by inclusion of 1 mM 5 (+) in the tissue extract prior to mixing with affinity resin. Mass spectrometry was used to identify the bound proteins. In lane E bound proteins were eluted with 25 mM sodium dithionite in phosphate buffered saline. Numbers indicate bands that were sequenced by MS; (1) Fatty acid synthase (2) Hsp90 (3) Hsp90 (4) Hsp90 proteolytic fragments.