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The effect of posttranslational modifications on biochemical and structural characteristics of Prion Protein variants and the SMN Tudor domain

The biochemical consequences of posttranslational modifications of different proteins were analyzed. A C-terminal membrane anchor influenced the biochemical/conformational properties of PrP variants and in vitro evidence for pore formation by one membrane-anchored PrP variant was found. SMN Tudor linked to its low affinity ligand symmetrically dimethylated arginine via different poly-glycine linkers demonstrated that covalent attachment can stabilize such weak interactions.