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Accepting its Random Coil Nature Allows a Partial NMR Assignment of the Neuronal Tau Protein
Author(s) -
Smet Caroline,
Leroy Arnaud,
Sillen Alain,
Wieruszeski JeanMichel,
Landrieu Isabelle,
Lippens Guy
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.200400145
Subject(s) - pairwise comparison , degeneracy (biology) , random coil , chemistry , gene isoform , protein secondary structure , computer science , bioinformatics , biochemistry , biology , artificial intelligence , gene
A combined strategy to obtain a partial NMR assignment of the neuronal Tau protein is presented. Confronted with the extreme spectral degeneracy that the spectrum of this 441 amino acid long unstructured protein presents, we have introduced a graphical procedure based on residue type‐specific product planes. Combining this strategy with the search for pairwise motifs, and combining the spectra of different Tau isoforms and even of peptides derived from the native sequence, we arrive at a partial assignment that is sufficient to map the interactions of Tau with its molecular partners. The obtained assignments equally confirm the absence of regular secondary structure in the isolated protein.