期刊
PROTEIN AND PEPTIDE LETTERS
卷 14, 期 1, 页码 87-91出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986607779117281
关键词
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
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [S06GM008205] Funding Source: NIH RePORTER
- NIGMS NIH HHS [S06 GM008205] Funding Source: Medline
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.
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