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The microtubule-associated protein tau is believed to be a natively unfolded molecule with virtually no secondary structure. However, this protein self-associates into filamentous forms in various neurodegenerative diseases. Since these filamentous forms show a remarkable degree of higher order due to their regular widths and periodicity, it is widely speculated that tau does contain secondary structures that come together to form tertiary and quaternary structures in the filamentous form. The purpose of this review is to use the primary sequence of tau along with predictive methods in an effort to identify potential secondary structural elements that could be involved in its normal and pathological functions. Although there are few predicted structural elements in the tau molecule, these analyses should lead to a better understanding of the structure/function relationships that regulate the behavior of tau.