The initial stages of amyloid fibrilization begin with the monomers populating aggregation-prone conformers. Characterization of such aggregation-prone conformers is crucial in the study of neurodegenerative diseases. The current study characterizes the aggregation pathway of two tau protein constructs that have been recently demonstrated to form Alzheimer's (AD) fibril structures with divalent ions and chronic traumatic encephalopathy (CTE) fibril structures with monovalent ions. The results highlight the involvement of identical residues in both the primary and secondary processes of both AD and CTE fibril propagation. Nuclear magnetic resonance relaxation experiments reveal increased flexibility of the motifs KCGS within R3 and PGGGN within R4 in the presence of MgCl/NaCl, correlating with faster aggregation kinetics and indicating efficient primary nucleation. Notably, the seeded aggregation kinetics of the tau monomers in the presence and absence of metal ions are strikingly different. This correlates with the overall sign of the NΔ profile specifying the dominant mechanism involved in the process of aggregation.