Protein Folding Using a Vortex Fluidic Device

Joshua Britton, Joshua Smith, Colin Raston, Gregory Weiss

    Research output: Chapter in Book/Report/Conference proceedingChapter

    Abstract

    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: Methods and Protocols
    PublisherSpringer
    Pages211-220
    Number of pages10
    Volume1586
    Edition2017
    ISBN (Print)9781493968879
    DOIs
    Publication statusPublished - 2017

    Publication series

    NameMethods in Molecular Biology
    Volume1586
    ISSN (Print)1064-3745

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  • Cite this

    Britton, J., Smith, J., Raston, C., & Weiss, G. (2017). Protein Folding Using a Vortex Fluidic Device. In Heterologous Gene Expression in E. coli: Methods and Protocols (2017 ed., Vol. 1586, pp. 211-220). (Methods in Molecular Biology; Vol. 1586). Springer. https://doi.org/10.1007/978-1-4939-6887-9_13