Effect of hyperphosphorylation on structure of TAU protein
Uverskiĭ, V.N.; Galzitskaia, O.V.; Winter, S.; Kittler, L.; Löber, G.
Tsitologiia 41(6): 540-549
1999
ISSN/ISBN: 0041-3771 PMID: 10505338 Document Number: 504287
Effect of hyperphosphorylation on structural properties and conformational stability of tau-protein was investigated by methods of circular dichroism and fluorescence decay. The normal protein displayed an unusual secondary structural elements--an extended left-handed helix. It is suggested that the structure of the normal tau-protein includes a globular C-terminal part with rigid extended tail, i.e., it is of a "tadpole" type. The normal protein structure is practically unaffected by changes in pH values. Hyperphosphorylation leads to some perturbation within the extended part of the protein molecule. Decrease in pH transforms the globular part of the hyperphosphorylated protein into the molten globule-like conformation.