期刊
JOURNAL OF BIOMOLECULAR NMR
卷 20, 期 1, 页码 11-14出版社
KLUWER ACADEMIC PUBL
DOI: 10.1023/A:1011258906244
关键词
protein G; protein stabilization; protein tag
资金
- NIGMS NIH HHS [P01 GM047467, GM 47467] Funding Source: Medline
Protein-fusion constructs have been used with great success for enhancing expression of soluble recombinant protein and as tags for affinity purification. Unfortunately the most popular tags, such as GST and MBP, are large, which hinders direct NMR studies of the fusion proteins. Cleavage of the fusion proteins often re-introduces problems with solubility and stability. Here we describe the use of N-terminally fused protein G (B1 domain) as a non-cleavable solubility-enhancement tag (SET) for structure determination of a dimeric protein complex. The SET enhances the solubility and stability of the fusion product dramatically while not interacting directly with the protein of interest. This approach can be used for structural characterization of poorly behaving protein systems, and would be especially useful for structural genomics studies.
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