Abstract
In vitro protein folding can be employed to produce complex proteins expressed as insoluble inclusion bodies in E. coli from laboratory to commercial scale. Often the most challenging step is identification of renaturation conditions that will enable the denatured protein to form the native structure at an acceptable yield. Generally this requires screening a matrix of buffers and stabilizers to find an appropriate solution. Herein, we describe an automated and quantitative method to identify optimal in vitro protein folding parameters with a high rate of success.
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Acknowledgments
We would like to acknowledge Alex Mladenovic and Randy Hecht for contributing to the construction and programming of the Biomek, Tom Boone for protein folding condition guidance and Jeff Lewis for expressing the recombinant protein described in this chapter.
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Walker, K.W., An, P., Winters, D. (2019). A High-Throughput Automated Protein Folding System. In: Vincentelli, R. (eds) High-Throughput Protein Production and Purification. Methods in Molecular Biology, vol 2025. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9624-7_6
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DOI: https://doi.org/10.1007/978-1-4939-9624-7_6
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