Premium
Hyperphosphorylation induces structural modification of tau‐protein
Author(s) -
Uversky Vladimir N,
Winter Stefan,
Galzitskaya Oxana V,
Kittler Leonhard,
Lober Gunter
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01303-9
Subject(s) - hyperphosphorylation , circular dichroism , chemistry , molten globule , biophysics , crystallography , protein structure , tau protein , molecule , globular protein , protein secondary structure , helix (gastropod) , biochemistry , phosphorylation , biology , snail , medicine , ecology , disease , organic chemistry , pathology , alzheimer's disease
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.