Figure 3: Conformational conversion of the EAQA peptide.
From: Design of protein switches based on an ensemble model of allostery
(a) α-Helical model of the WA-(EAQA)n peptide structure, (b) with isoelectric points and dimensions for two- to four-coiled α-helical structures: (EAQA)2–4 and a cross-sectional view, showing side-chain residues. (c) MD simulation of the α-helical model of (EAQA)3 peptide with increasing pH: pH 3 (black), pH 5 (blue) and pH 7 (red). Backbone r.m.s.d. relative to the initial structure as a function of simulation time at 300 K and (d) final structures after 10, 50 and 100-ns simulation. (e) CD spectra and (f) fluorescence emission spectra of WA-(EAQA)7 at pH 4.5 (solid line), pH 5.5 (dashed line), pH 6.5 (dash-dotted line) and pH 7.5 (dotted lines).
