One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester
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چکیده
منابع مشابه
One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester
BACKGROUND Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester. This uniquely reactive C-terminus can be used in native chemical ligation reactions to introduce synthetic groups or to immobilize proteins on surfaces and nanoparticles. Unfortunately, common refolding procedures for recombinant proteins that contain di...
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15 صفحه اولRefolding Process of Cysteine-Rich Proteins: Chitinase as a Model
Background: Recombinant proteins overexpressed in E. coli are usually deposited in inclusion bodies. Cysteines in the protein contribute to this process. Inter- and intra- molecular disulfide bonds in chitinase, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed in E. coli. Hence, aggregated proteins should be solubilized and allowed to refold to obtain nat...
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ژورنال
عنوان ژورنال: BMC Biotechnology
سال: 2008
ISSN: 1472-6750
DOI: 10.1186/1472-6750-8-76