Hyperphosphorylation Induces Structural Modification of Tau-protein
Document Type
Article
Publication Date
1998
Digital Object Identifier (DOI)
https://doi.org/10.1016/S0014-5793(98)01303-9
Abstract
The effect of hyperphosphorylation on the structural properties and conformational stability of bovine tau-protein was studied by means of circular dichroism and fluorescence lifetime techniques. Normal protein contains unusual secondary structure elements: extended left-handed helices. The structure of this protein was assumed to be of a ‘tadpole’ type – a globular C-terminal part with a long and rigid tail included in the extended left-handed helix. Either a decrease or an increase of pH induced only minor changes of the normal tau-protein surface. Hyperphosphorylation affected the extended part of the protein molecule; the decrease of pH in this case induced considerable structural rearrangements, and the conformation of the C-terminal part of the protein molecule was transformed into a molten globule-like state.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 439, issue 1-2, p. 21-25
Scholar Commons Citation
Uversky, Vladimir N.; Winter, Stefan; Galzitskaya, Oxana V.; Kittler, Leonhard; Loberg, Harmonie; and Lober, Gunter, "Hyperphosphorylation Induces Structural Modification of Tau-protein" (1998). Molecular Medicine Faculty Publications. 649.
https://digitalcommons.usf.edu/mme_facpub/649
