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- W2389367637 abstract "Highly purified soluble proteins with bioactivities are the bases for structural and functional studies of protein,and obtaining such samples has long been a desired goal for researchers in the field of molecular and structural biology.However,through usual expression methods,heterologous recombinant proteins are often unable to fold correctly to bioactive conformation,resulting in the difficulties in high-efficient expression.This paper reviews the molecular mechanisms and the current applications of molecular chaperone-assisted expression of recombinant protein.Some existing problems and related solving strategies,including the selection principles of the molecular chaperone and the correlation between protein expression systems and the molecular chaperones,were discussed.Hopefully this review may serve as a reference for rationally utilizing the molecular chaperone in the research of recombinant protein expression." @default.
- W2389367637 created "2016-06-24" @default.
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- W2389367637 date "2012-01-01" @default.
- W2389367637 modified "2023-09-24" @default.
- W2389367637 title "Research progresses of high-efficient expression of recombinant protein assisted by molecular chaperone" @default.
- W2389367637 hasPublicationYear "2012" @default.
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