Abstract
Post-translational modifications (PTMs) are important for regulating protein activity, intramolecular structure, intermolecular interaction, and localization. PTMs within the first 17 amino acids (Nt17) of the Huntingtin protein (Htt) have been shown to influence the aggregation and toxicity of mutant Htt proteins in vitro and in various cellular/neuronal models of Huntington’s disease. However, the structural basis underlying how PTMs influence aggregation at a microscopic level is missing.
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