Studying the Natively Unfolded Neuronal Tau Protein by Solution NMR Spectroscopy

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Abstract:

The neuronal Tau protein, whose physiological role is to stabilize the microtubules, is found under the form of aggregated filaments and tangles in Alzheimer's diseased neurons. Until recently detailed structural analysis of the natively unfolded Tau protein has been hindered due to its shear size and unfavourable amino acid composition. We review here the recent progress in the assignments of the full-length polypeptide using novel methods of product planes and peptide NMR mapping, and indicate the structural insights that can be obtained from this assignment. Preliminary NMR data on the fibers show that the assignment enables a precise mapping of the rigid core. Future NMR experiments should allow one to gain more insight into the conformational aspects of this intriguing protein.





Keywords: Alzheimer's disease; NMR spectroscopy; natively unfolded protein; paired helical fragment; tau protein

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606775338461

Affiliations: Institut de Biologie de Lille, Institut Pasteur de Lille, UMR CNRS 8525, BP 245, F-59019 Lille Cedex, France.

Publication date: March 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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