Studying the Natively Unfolded Neuronal Tau Protein by Solution NMR Spectroscopy

Title: Studying the Natively Unfolded Neuronal Tau Protein by Solution NMR Spectroscopy

Volume: 13 Issue: 3

Author(s): Guy Lippens, Alain Sillen, Caroline Smet, Jean-Michel Wieruszeski, Arnaud Leroy, Luc Buee and Isabelle Landrieu

Affiliation:

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

Abstract: The neuronal Tau protein, whose physiological role is to stabilize the microtubules, is found under the form of aggregated filaments and tangles in Alzheimers 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.

Cite this article as:

Lippens Guy, Sillen Alain, Smet Caroline, Wieruszeski Jean-Michel, Leroy Arnaud, Buee Luc and Landrieu Isabelle, Studying the Natively Unfolded Neuronal Tau Protein by Solution NMR Spectroscopy, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338461