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Updated: Sep 24, 2026

In vitro Methylation Assay to Study Protein Arginine Methylation
Published on: October 5, 2014
Chemical basis for arginine citrullination by human PAD4
Nurgül Bilgin1, Laust Moesgaard1, Jacob Kongsted1
1Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230, Odense, Denmark. kongsted@sdu.dk.
Abstract:
Peptidyl arginine deiminase 4 (PAD4)-catalysed citrullination of arginine residues in histone proteins plays an important role in eukaryotic gene regulation. Enzyme assays with histone H4 peptides possessing the simplest arginine mimics demonstrate that human PAD4 exhibits narrow substrate selectivity. Computational analyses reveal that the arginine substrate recognition is governed by strong noncovalent interactions with PAD4 and energetically favourable desolvation of the PAD4 active site.
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