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.