Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites.
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.
Lippens
Guy
G
CNRS-Université de Lille 2 UMR 8525, Institut Pasteur de Lille, BP 245 59019 Lille Cedex, France. Guy.Lippens@pasteur-lille.fr
Wieruszeski
Jean-Michel
JM
Leroy
Arnaud
A
Smet
Caroline
C
Sillen
Alain
A
Buée
Luc
L
Landrieu
Isabelle
I
D000596:Amino Acids / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009584:Nitrogen / Q000737:chemistry; D010766:Phosphorylation; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D016875:tau Proteins / Q000096:biosynthesis / Q000737:chemistry*
D000596:Amino Acids; D011994:Recombinant Proteins; D016875:tau Proteins; D011392:Proline; D009584:Nitrogen