Secondary structural preference of tau in each of the systems (Table 2 ) shows random coil is the most preferred confirmation. All five system has more than sixty percent of the amino acids in a random coil state. The maximum number of beta sheets are found in the glycosylated tau (Tau_glyc) form, i.e., 4 %, followed by phosphorylated (Tau_phos) tau form (3%), while in Tau_plane percent of beta sheet is as low as 1%. The percentage of beta bridges are more in phosphorylated tau (Tau_phos), followed by glycosylated tau. Bend confirmation is the second most preferred state in all systems throughout the trajectory, with each system having close to 20 % amino acids in bend form. Turns and alpha helix are highest in Tau_plane, other systems have fewer turns and negligible helix forms. The secondary structure analysis indicates that the glycosylated form of tau shows the maximum preference to beta sheet confirmations, followed by the phosphorylated tau (Tau_phos). The unmodified tau protein shows a very low beta sheet propensity. This indicates that glycosylated tau have a high aggregation tendency as indicated by its high beta sheet content. It is also worth mentioning that, apart from the intra molecular beta sheets that we analyzed from the simulation trajectories, tau fibril formation & aggregation also depends on various inter molecular beta sheet formations which are formed as a result of the interaction of more than one tau protein during the aggregation process, which could not be sampled as we were studying only a single tau peptide.