Mass spectrometry data confirming tetrameric α-synuclein N-terminal acetylation
Ricardo D Fernández1, Heather R Lucas1
1Department of Chemistry, Virginia Commonwealth University, Richmond, VA, USA.
Abstract:
Tetrameric α-synuclein (αS) is an elusive multimer of the dynamic neuronal protein implicated in Parkinson׳s disease. Through the data reported herein, we demonstrate that this high molecular weight multimer is N-acetylated. Coexpression of tetrameric αS in Escherichia coli with the NatB acetylase derived from yeast enables access to N-terminally acetylated αS (NAcαS), the native form in humans. Following purification and characterization as previously described by us in "Isolation of Recombinant Tetrameric N-acetylated α-synuclein" (Fernández and Lucas, 2018), the purified protein was excised from a native gel for confirmation of N-terminal acetylation. Through high-resolution mass spectrometry techniques, the identification of this helical tetramer as NAcαS has been clearly demonstrated.
More Related Videos
09:09Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics
Published on: October 13, 2020
08:40Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
Published on: June 23, 2022
Related Concept Videos
Mass Spectrometry: Overview
Tandem Mass Spectrometry
Mass Spectrometry: Isotope Effect
Mass Spectrometry of Amines
Confirmation Biases
Chemical Ionization (CI) Mass Spectrometry
