The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated

Escherichia coli maltose binding protein (MBP) is commonly used to promote the solubility of its fusion partners. To investigate the mechanism of solubility enhancement by MBP, we compared the properties of MBP fusion proteins refolded in vitro with those of the corresponding fusion proteins purifie...

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Veröffentlicht in:PloS one 2012-11, Vol.7 (11), p.e49589-e49589
Hauptverfasser: Raran-Kurussi, Sreejith, Waugh, David S
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Sprache:eng
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