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pubmed-article:14695515pubmed:abstractTextNMR 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.lld:pubmed
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pubmed-article:14695515pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:14695515pubmed:articleTitleProline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites.lld:pubmed
pubmed-article:14695515pubmed:affiliationCNRS-Université de Lille 2 UMR 8525, Institut Pasteur de Lille, BP 245 59019 Lille Cedex, France. Guy.Lippens@pasteur-lille.frlld:pubmed
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