Solvent accessible surface area
Hydrophobic interactions of amino acids at the core of the protein plays important role in the protein folding process. As the core hydrophobic interactions get buried inside the compact protein, the surface of the protein exposed to the solvent decrease since only polar amino acids at the surface makes contact with the solvent. Hence, solvent accessible surface area (SASA) analysis of proteins help to understand the surface area of proteins that are interacting with the solvent, and the stability of the hydrophobic core [14, 40]. The total SASA of each system were analyzed and plotted (Figure 1 E) . We can see that SASA of each system gets stabilized after the first 100 ns, while Tau_plane shows maximum deviations and remains high for most of the simulation. Tau_phos shows the least deviations while Tau_glyc sasa is relatively stable and low as compared to Tau_plane. The average SASA values indicate that Tau_phos have the lowest SASA (38.9 nm2), followed by Tau_glyc (44.9 nm2), while SASA for Tau_plane (48.7 nm2) remains high (Table 1) . The probability distribution graphs for radius of gyration, end to end distance and solvent accessible surface have been incorporated in supporting information along with representative extended and compact conformations of the peptide in each system in Figure S1 and S2 respectively.