Hyperphosphorylation induces structural modification of tau‐protein

FEBS Letters

Lober, Gunter³  Galzitskaya, Oxana V³  Winter, Stefan²  Kittler, Leonhard²  Uversky, Vladimir N¹ 

[1] Institute for Biological Instrumentation, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia;Institute for Molecular Biotechnology, 100813, D-07708 Jena, Germany;Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia

关键词: Tau-protein;    Molten globule;    Protein structure and stability;    Conformational change;   

DOI  :  10.1016/S0014-5793(98)01303-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown