Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategy

Lashuel, HilalAnsaloni, Annalisa2014-04-222014-04-22201410.5075/epfl-thesis-6188https://infoscience.epfl.ch/handle/20.500.14299/102920urn:nbn:ch:bel-epfl-thesis6188-1enHuntington’s disease (HD)Huntingtin exon1 (Httex1)N-terminal 17 domain (Nt17)aggregationoligomersphosphorylationPost Translational Modifications (PTMs)protein semisynthesisSolid-Phase Peptide Synthesis (SPPS)Native Chemical Ligation (NCL)Expressed Protein Ligation (EPL)Transmission Electron Microscopy (TEM)Atomic Force Microscopy (AFM)Nuclear Magnetic Resonance (NMR)Circular Dichroism (CD)Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategythesis::doctoral thesis