Significant enhanced expression and solubility of human proteins in Escherichia coli by fusion with protein S from Myxococcus xanthus
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Noncognate Mycobacterium tuberculosis toxin-antitoxins can physically and functionally interactSegmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubilitySweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression.Latest approaches for efficient protein production in drug discovery.An endogenous protein inhibitor, YjhX (TopAI), for topoisomerase I from Escherichia coli.Suppression of the toxicity of Bac7 (1-35), a bovine peptide antibiotic, and its production in E. coli.Characterization of YjjJ toxin of Escherichia coli.Expression of cold-adapted β-1,3-xylanase as a fusion protein with a ProS2 tag and purification using immobilized metal affinity chromatography with a high concentration of ArgHCl.
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P2860
Significant enhanced expression and solubility of human proteins in Escherichia coli by fusion with protein S from Myxococcus xanthus
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 19 June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Significant enhanced expressio ...... tein S from Myxococcus xanthus
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Significant enhanced expressio ...... ein S from Myxococcus xanthus.
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type
label
Significant enhanced expressio ...... tein S from Myxococcus xanthus
@en
Significant enhanced expressio ...... ein S from Myxococcus xanthus.
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prefLabel
Significant enhanced expressio ...... tein S from Myxococcus xanthus
@en
Significant enhanced expressio ...... ein S from Myxococcus xanthus.
@nl
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Significant enhanced expressio ...... tein S from Myxococcus xanthus
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Hiroshi Kobayashi
Masayori Inouye
Takeshi Yoshida
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10.1128/AEM.00691-09
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P577
2009-06-19T00:00:00Z