Accepting its random coil nature allows a partial NMR assignment of the neuronal Tau protein.
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.
Smet
Caroline
C
CNRS--Université de Lille 2, UMR 8525, Institut Pasteur de Lille, B. P. 245, 59019 Lille, France.
Leroy
Arnaud
A
Sillen
Alain
A
Wieruszeski
Jean-Michel
JM
Landrieu
Isabelle
I
Lippens
Guy
G
D000595:Amino Acid Sequence; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009474:Neurons / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism
D010446:Peptide Fragments; D011994:Recombinant Proteins; D016875:tau Proteins