Hyperphosphorylation induces structural modification of tau-protein.
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.
Uversky
V N
VN
Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region. uversky@vega.protres.ru
Winter
S
S
Galzitskaya
O V
OV
Kittler
L
L
Lober
G
G
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
D016875:tau Proteins