Protein Folding Using a Vortex Fluidic Device

Joshua Britton, Joshua N. Smith, Colin L. Raston, Gregory A. Weiss

    Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

    2 Citations (Scopus)


    Essentially all biochemistry and most molecular biology experiments require recombinant proteins. However, large, hydrophobic proteins typically aggregate into insoluble and misfolded species, and are directed into inclusion bodies. Current techniques to fold proteins recovered from inclusion bodies rely on denaturation followed by dialysis or rapid dilution. Such approaches can be time consuming, wasteful, and inefficient. Here, we describe rapid protein folding using a vortex fluidic device (VFD). This process uses mechanical energy introduced into thin films to rapidly and efficiently fold proteins. With the VFD in continuous flow mode, large volumes of protein solution can be processed per day with 100-fold reductions in both folding times and buffer volumes.

    Original languageEnglish
    Title of host publicationHeterologous Gene Expression in E. coli
    Subtitle of host publicationMethods and Protocols
    Place of PublicationNew York
    Number of pages10
    ISBN (Electronic)9781493968879
    ISBN (Print)9781493968855
    Publication statusE-pub ahead of print - 4 May 2017

    Publication series

    NameMethods in Molecular Biology
    ISSN (Print)1064-3745


    • Bacterial protein expression
    • Continuous flow
    • Inclusion bodies
    • Misfolded proteins
    • Protein folding
    • Vortex fluidics


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