In humans, brain connections are usually strengthened using a microtubule-associated protein called Tau, but that function diminishes with old age. Aging may cause disruption of normal physiological processes and create a disease such as Alzheimer’s as a direct result. Understanding the characteristics of Tau is important as it is implicated in neurofibrillary tangles, one of the main symptoms of Alzheimer’s disease. Our interests delve into understanding the relationship between Tau and microtubules in order to know the role Tau’s shape and function have during its interactions with microtubules. Characterization of Tau may provide insight on how adjustment of its form can prevent symptoms of Alzheimer’s disease. This project examines the traits of a newly made type of Tau and endeavors to understand the traits of the protein by expressing segments of it and comparing the microtubule interactions. Assays have determined the binding affinity of certain Tau constructs thought to have physiological relevance, and microscopy visualized and compared assembled Tau-mediated microtubule bundles for differences in formation. Results show that Tau is important in the microtubule assembly process, and that it is necessary in neuronal expression. These results justify extensive comparison amongst many variants of Tau to determine which form exceeds the current benchmark of the microtubule assembly processes.