title: Hyperphosphorylation induces structural modification of tau-protein.
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.
authors.affiliation: Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region. uversky@vega.protres.ru
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
authors.forename: S
authors.initials: S
authors.lastname: Winter
authors.forename: O V
authors.initials: OV
authors.lastname: Galzitskaya
authors.forename: L
authors.initials: L
authors.lastname: Kittler
authors.forename: G
authors.initials: G
authors.lastname: Lober
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D016875:tau Proteins