[Effect of hyperphosphorylation on structure of TAU protein].
Effect of hyperphosphorylation on structural properties and conformational stability of tau-protein was investigated by methods of circular dichroism and fluorescence decay. The normal protein displayed an unusual secondary structural elements--an extended left-handed helix. It is suggested that the structure of the normal tau-protein includes a globular C-terminal part with rigid extended tail, i.e., it is of a "tadpole" type. The normal protein structure is practically unaffected by changes in pH values. Hyperphosphorylation leads to some perturbation within the extended part of the protein molecule. Decrease in pH transforms the globular part of the hyperphosphorylated protein into the molten globule-like conformation.
Uverskiĭ
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VN
Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino.
Galzitskaia
O V
OV
Winter
S
S
Kittler
L
L
Löber
G
G
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D008870:Microtubules / Q000378:metabolism; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism
D016875:tau Proteins