Fig. 3
The simulated peptide is linear and mostly unstructured. a Stacked bar chart labelled with amino acid one-letter codes showing the per-residue structure content that is mostly random coil. b The time series of Rg shows that after 40 ns of equilibration, the peptide maintains a single length. c Time series of the vector angle between the first principal axis and the dipole moment created by the charged residues. This shows that the dipole is closely aligned to the long axis of the peptide. d Net charge of the peptide across a range of pH values. All residues in the charged region are charged between approximately pH 5–10, leading to a net charge of −4 e. e Space-filling model of a representative structure of the FLAG-tag peptide, showing the turn across residues F2–A7, and the extended random coil structure of the polar, charged residues (D16–K21). Scale bar: 1 nm
