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. Author manuscript; available in PMC: 2016 Nov 1.
Published in final edited form as: Biochim Biophys Acta. 2015 Sep 2;1848(11 0 0):2767–2778. doi: 10.1016/j.bbamem.2015.09.003

Figure 3.

Figure 3

Schematic representations of tilt angles for WT and mutant peptides in AT simulations. Top: WT peptide. Small grey boxes at the tip of the vertical bars indicate the mean z-position of the Lys Cγ atom. To represent the Cγ positions in 3-dimensions, grey vertical lines were anchored to the horizontal plane that represents the height of the COM for the peptide. The root positions of the bars are not accurate, but indicate that K8, K28, K25, K22 and K20 are arrayed in a counterclockwise order when viewed from the bottom, and that K22 and K15 are located somewhat internally compared to K20 and K25. The remaining figures: Results for each mutant are indicated by red and blue arrows that are superimposed on the WT data. Arrows start from the Cγ position observed for WT (i.e., grey boxes) and end at the positions observed in the simulation of each mutant. Red and blue colors indicate increase and decrease, respectively, in the z-position relative to the position in WT. Bold numbers denote native residues, whereas encircled numbers denote mutated residues.