Tau protein plays an essential role in maintaining the stability of neuronal microtubules. However, when excessively phosphorylated, particularly at serine and threonine residues, it is believed to contribute significantly to the development of Alzheimer’s disease. These post-translational modifications can lead to substantial changes in the three-dimensional conformation and physicochemical behavior of the protein. The present study investigates the hypothesis that different phosphorylation states of Tau generate distinct three-dimensional surface patterns, which can be identified and characterized through geometric descriptors and unsupervised clustering techniques. Two independent datasets were analyzed. The first dataset, used primarily for exploratory analysis, included nine progressively phosphorylated states of Tau protein, with modifications limited to serine residues.