Rapid protein-folding assay using green fluorescent protein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-07

AUTHORS

G S Waldo, B M Standish, J Berendzen, T C Terwilliger

ABSTRACT

Formation of the chromophore of green fluorescent protein (GFP) depends on the correct folding of the protein. We constructed a "folding reporter" vector, in which a test protein is expressed as an N-terminal fusion with GFP. Using a test panel of 20 proteins, we demonstrated that the fluorescence of Escherichia coli cells expressing such GFP fusions is related to the productive folding of the upstream protein domains expressed alone. We used this fluorescent indicator of protein folding to evolve proteins that are normally prone to aggregation during expression in E. coli into closely related proteins that fold robustly and are fully soluble and functional. This approach to improving protein folding does not require functional assays for the protein of interest and provides a simple route to improving protein folding and expression by directed evolution. More... »

PAGES

691-695

Journal

TITLE

Nature Biotechnology

ISSUE

7

VOLUME

17

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/10904

    DOI

    http://dx.doi.org/10.1038/10904

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1038056819

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10404163


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