Abstract
Post-translational modifications (PTMs) of proteins modulate folding, alter stability, and change interactions with ligands and are thus a primary feature of cell signaling pathways. PTMs can exist as covalent amino acid side chain modifications or alterations to the length and composition of the polypeptide chain termini. Here we probe the effect of PTMs on α-synuclein (αSyn) voltage-induced interactions with the voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane. The divalent Alexa Fluor 488 sidechain was attached separately at two positions on the αSyn C-terminal domain and serves as a PTM mimic.
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