In neurons, the microtubule associated protein, tau, is found in the axons. Tau stabilizes the microtubules required for neurotransmitter transport to the axonal terminal. Since tau has been found in both Alzheimer neurofibrillary tangles (NFT) and in paired helical filaments (PHF), the study of tau's normal structure had to preceed TEM studies of NFT and PHF. The structure of tau was first studied by ultracentrifugation. This work suggested that it was a rod shaped molecule with an axial ratio of 20:1. More recently, paraciystals of phosphorylated and nonphosphoiylated tau have been reported. Phosphorylated tau was 90-95 nm in length and 3-6 nm in diameter where as nonphosphorylated tau was 69-75 nm in length. A shorter length of 30 nm was reported for undamaged tau indicating that it is an extremely flexible molecule. Tau was also studied in relation to microtubules, and its length was found to be 56.1±14.1 nm.
A new look at the decomposition of unipotents and the normal structure of Chevalley groups
