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|Title:||Thermostable exoshells fold and stabilize recombinant proteins||Authors:||Deshpande, Siddharth
Masurkar, Nihar D.
Girish, Vallerinteavide Mavelli
Chan, Juliana M.
Drum, Chester L.
|Issue Date:||2017||Source:||Deshpande, S., Masurkar, N. D., Girish, V. M., Desai, M., Chakraborty, G., Chan, J. M., et al. (2017). Thermostable exoshells fold and stabilize recombinant proteins. Nature Communications, 8(1), 1442-.||Series/Report no.:||Nature Communications||Abstract:||The expression and stabilization of recombinant proteins is fundamental to basic and applied biology. Here we have engineered a thermostable protein nanoparticle (tES) to improve both expression and stabilization of recombinant proteins using this technology. tES provides steric accommodation and charge complementation to green fluorescent protein (GFPuv), horseradish peroxidase (HRPc), and Renilla luciferase (rLuc), improving the yields of functional in vitro folding by ~100-fold. Encapsulated enzymes retain the ability to metabolize small-molecule substrates, presumably via four 4.5-nm pores present in the tES shell. GFPuv exhibits no spectral shifts in fluorescence compared to a nonencapsulated control. Thermolabile proteins internalized by tES are resistant to thermal, organic, chaotropic, and proteolytic denaturation and can be released from the tES assembly with mild pH titration followed by proteolysis.||URI:||https://hdl.handle.net/10356/89629
|DOI:||10.1038/s41467-017-01585-2||Rights:||© 2017 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SCBE Journal Articles|
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