Abstract
Due to asymmetrical charge distribution of the mammalian high mobility group protein A2 (HMGA2), which makes HMGA2 bind to both cation- and anion-exchange columns, we developed a rapid procedure for purifying HMGA2 in the milligram range. This purification procedure greatly facilitated biophysical studies, which require large amounts of the protein.
Keywords: The mammalian high mobility group protein A2 (HMGA2), DNA binding protein, isothermal titration calorimetry, differential scanning calorimetry, nuclear magnetic resonance (NMR) Spectroscopy, intrinsically unstructured protein