LAUSR

α-Synuclein (αS) is an abundant neuronal protein implicated in Parkinson's disease. Acetylation of the N-terminal methionine of αS is a ubiquitous modification of αS derived from healthy brain tissue as well as from Parkinson's disease patients. In vitro, it has a minor impact on both the solution structure and membrane-binding properties of αS and its role in αS function is unknown. In order to gain greater insight into the role N-terminal acetylation in αS function, we created an acetylation mimic, where the N-terminal methionine is replaced with asparagine (αSasn) and contrasted it with unmodified (αSunmod) and N-terminally acetylated (αSacetyl ) αS.