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. Author manuscript; available in PMC: 2014 Nov 5.
Published in final edited form as: Biochemistry. 2013 Oct 23;52(44):7818–7829. doi: 10.1021/bi401106b

Figure 5.

Figure 5

c(s) distributions of the catalytic domain of AMSH binding to (a) the SH3 domain of STAM and (b) UIM-SH3. Three concentration series were used to assess the formation of the AMSH:SH3 and AMSH:UIM-SH3 complexes revealing 1:1 complexes at 2.5S and 2.6S, respectively. Excess SH3 and UIM-SH3 are present at 1.3S. The data for both c(s) distributions were normalized to the peak area of the complexes. (C) Overlay of AMSH, AMSH:SH3, and AMSH:UIM-SH3 revealing changes in s-value of the AMSH:SH3 and AMSH:UIM-SH3 complexes compared to AMSH alone at 2.2S. The c(s) distributions were normalized to the peak area of the complexes.