Journal
CHEMBIOCHEM
Volume 5, Issue 12, Pages 1639-1646Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200400145
Keywords
neuronal Tau protein; NMR spectroscopy; peptide mapping; protein folding; protein structures
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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.
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