Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategy
2014
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Title
Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategy
Author(s)
Ansaloni, Annalisa
Advisor(s)
Date
2014
Publisher
Lausanne, EPFL
Keywords
Huntington’s disease (HD); Huntingtin exon1 (Httex1); N-terminal 17 domain (Nt17); aggregation; oligomers; phosphorylation; Post Translational Modifications (PTMs); protein semisynthesis; Solid-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)
Language
English
Other identifier(s)
urn: urn:nbn:ch:bel-epfl-thesis6188-1
Laboratories
LMNN
Record Appears in
Scientific production and competences > SV - School of Life Sciences > BMI - Brain Mind Institute > LMNN - Laboratory of Molecular Neurobiology and Neuroproteomics
Scientific production and competences > EPFL Theses
Work produced at EPFL
Published
Theses
Scientific production and competences > EPFL Theses
Work produced at EPFL
Published
Theses
Record creation date
2014-04-22