Figure 2: Close contact maps of the five simulated systems, indicating average residue-residue close contacts across the trajectory. Tau_glyc and Tau_phos show residue-residue close contacts, while the unmodified tau (Tau_plane) shows negligible inter-residue close contacts.
We can see that in Tau_plane, the average inter-residue close contacts are negligible, indicating the protein is making very few inter-residue close contacts, and most likely to exist in an extended confirmation as a folded conformation is likely to have inter-residue interactions. But in Tau_glyc, residue Lys343-Gly355 is making close contact with residues Glu372-Glu380. This shows that the two ends of the protein are more likely to be in close contact, and might be existing in a collapsed/folded conformation than an extended form. A similar trend is visible in Tau_phos in which residues Lys347-Ser356 are in close contact with residues Ile371-Glu380. Tau_p356 forms negligible close contacts between residues Ile354-Ser356 with Leu376-Glu380 and Lys340-Lys341 with Gly355-Ser356-17. Tau_p352, like Tau_plane form negligible close contacts.