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Proline‐Directed Random‐Coil Chemical Shift Values as a Tool for the NMR Assignment of the Tau Phosphorylation Sites
Author(s) -
Lippens Guy,
Wieruszeski JeanMichel,
Leroy Arnaud,
Smet Caroline,
Sillen Alain,
Buée Luc,
Landrieu Isabelle
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300763
Subject(s) - phosphorylation , random coil , nuclear magnetic resonance spectroscopy , proline , chemistry , residue (chemistry) , amino acid , amino acid residue , chemical shift , stereochemistry , biochemistry , peptide sequence , circular dichroism , gene
NMR spectroscopy of the full‐length neuronal Tau protein has proved to be difficult due to the length of the protein and the unfavorable amino acid composition. We show that the random‐coil chemical shift values and their dependence on the presence of a proline residue in the ( i +1) position can successfully be exploited to assign all proline‐directed phosphorylation sites. This is a first step toward the study of the phosphorylation of Tau by NMR spectroscopy.