HR α-helix wheel and interaction prediction.

<p>(a) Standard heptad repeat motif has interaction and solvent-accessible sites. (b) In the heptad repeat of α-helix wheel, positions <i>a, d</i> and <i>e</i> are the interactive sites and positions <i>b, c, f,</i> and <i>g</i> are the solvent-accessible sites. (c) Amino acid sequences of the three peptides and corresponding EK modified peptides with underlines are <i>a, d,</i> and <i>e</i> sites, respectively. (d) Predict-protein computational (<a href="https://www.predictprotein.org" target="_blank">https://www.predictprotein.org</a>) was used to predict the tendency to form complex for mixed peptides in pairs. The tendency of gHH1 and gBH1 to form complex is 52.5%, of gHH1 and gHH3 is 44.8%, and of gBH1 and gHH3 is 64.7%.