The structure of pathogenic huntingtin exon-1 defines the bases of its aggregation propensity
C. A. Elena-Real, A. Sagar, A. Urbanek, M. Popovic, A. Morato, A. Estana, A. Fournet, X. L. Lund, Z.-D. Shi, L. Costa, A. Thureau, F. Allemand, R. E. Swenson, P.-E. Milhiet, A. Barducci, , P. Bernado
This study investigates how the structure of pathogenic huntingtin exon-1 with expanded poly-Q tracts influences its aggregation propensity and fibril formation.
bioRxiv · Oct 25, 2022Biophysics