Crystal structures of MBP fusion proteins
نویسندگان
چکیده
منابع مشابه
Crystal structures of fusion proteins with large-affinity tags.
The fusion of a protein of interest to a large-affinity tag, such as the maltose-binding protein (MBP), thioredoxin (TRX), or glutathione-S-transferase (GST), can be advantageous in terms of increased expression, enhanced solubility, protection from proteolysis, improved folding, and protein purification via affinity chromatography. Unfortunately, crystal growth is hindered by the conformationa...
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متن کاملCABM Symposium Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
It is difficult to imagine any strategy for high-throughput protein expression and purification that does not involve genetically engineered affinity tags. Because of its ability to enhance the solubility and promote the proper folding of its fusion partners, Escherichia coli maltose-binding protein (MBP) is a particularly useful affinity tag. However, not all MBP fusion proteins bind efficient...
متن کاملUse of a 96-well format for the affinity purification of maltose-binding protein (MBP) fusion proteins.
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Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli.
Many proteins that accumulate in the form of insoluble aggregates when they are overproduced in Escherichia coli can be rendered soluble by fusing them to E. coli maltose binding protein (MBP), and this will often enable them to fold in to their biologically active conformations. Yet, although it is an excellent solubility enhancer, MBP is not a particularly good affinity tag for protein purifi...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2016
ISSN: 0961-8368
DOI: 10.1002/pro.2863