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. 2014 Mar 4;9(3):e90889. doi: 10.1371/journal.pone.0090889

Figure 5. Binding requirements of the SMRT peptide explored utilising artificial amino acids to replace histidine.

Figure 5

(A) Binding curves obtained by fluorescence polarisation for wild-type peptide and 1-napthyl, 2-napthyl, styryl and homophenylalanine substitutions of histidine1426 of SMRT. The Kd in µM (mean±SEM) is presented to the right of the compound name. (B) Structure of wild-type SMRT peptide bound to the BCL6-POZ domain. Molecular modelling of (C) 1-naphthyl SMRT peptide and (D) 2-naphthyl SMRT peptide.