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Large Scale Preparation of the Mammalian High Mobility Group Protein A2 for Biophysical Studies

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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: DNA binding protein; The mammalian high mobility group protein A2 (HMGA2); differential scanning calorimetry; intrinsically unstructured protein; isothermal titration calorimetry; nuclear magnetic resonance (NMR) Spectroscopy

Document Type: Research Article


Affiliations: Department of Chemistry and Biochemistry, Florida International University, 11200 SW 8th Street, Miami,Florida 33199, USA.

Publication date: January 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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