Hyperphosphorylation induces structural modification of tau-protein.

V N Uversky; S Winter; O V Galzitskaya; L Kittler; G Lober

doi:10.1016/s0014-5793(98)01303-9

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Hyperphosphorylation induces structural modification of tau-protein.

V N Uversky·S Winter·O V Galzitskaya·L Kittler·G Lober

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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.

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Animals Cattle Circular Dichroism Hydrogen-Ion Concentration Phosphorylation Protein Structure, Secondary Spectrophotometry, Ultraviolet tau Proteins Journal Article Research Support, Non-U.S. Gov't

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V N Uversky, S Winter, O V Galzitskaya, L Kittler, G Lober. 1998-11-13. Hyperphosphorylation induces structural modification of tau-protein.. https://doi.org/10.1016/s0014-5793(98)01303-9

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