Thermostable exoshells fold and stabilize recombinant proteins

Improving recombinant protein expression and stabilization remains a significant challenge. Here, the authors engineer Archaeoglobus fulgidus ferritin as a thermostable exoshell to provide steric accommodation and charge complementation for recombinant proteins, which can improve yields by 100 fold.

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Autores principales:	Siddharth Deshpande, Nihar D. Masurkar, Vallerinteavide Mavelli Girish, Malan Desai, Goutam Chakraborty, Juliana M. Chan, Chester L. Drum
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8a4348c6e72946be878fa93b29252878
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spelling	oai:doaj.org-article:8a4348c6e72946be878fa93b292528782021-12-02T17:06:18ZThermostable exoshells fold and stabilize recombinant proteins10.1038/s41467-017-01585-22041-1723https://doaj.org/article/8a4348c6e72946be878fa93b292528782017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01585-2https://doaj.org/toc/2041-1723Improving recombinant protein expression and stabilization remains a significant challenge. Here, the authors engineer Archaeoglobus fulgidus ferritin as a thermostable exoshell to provide steric accommodation and charge complementation for recombinant proteins, which can improve yields by 100 fold.Siddharth DeshpandeNihar D. MasurkarVallerinteavide Mavelli GirishMalan DesaiGoutam ChakrabortyJuliana M. ChanChester L. DrumNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Siddharth Deshpande Nihar D. Masurkar Vallerinteavide Mavelli Girish Malan Desai Goutam Chakraborty Juliana M. Chan Chester L. Drum Thermostable exoshells fold and stabilize recombinant proteins
description	Improving recombinant protein expression and stabilization remains a significant challenge. Here, the authors engineer Archaeoglobus fulgidus ferritin as a thermostable exoshell to provide steric accommodation and charge complementation for recombinant proteins, which can improve yields by 100 fold.
format	article
author	Siddharth Deshpande Nihar D. Masurkar Vallerinteavide Mavelli Girish Malan Desai Goutam Chakraborty Juliana M. Chan Chester L. Drum
author_facet	Siddharth Deshpande Nihar D. Masurkar Vallerinteavide Mavelli Girish Malan Desai Goutam Chakraborty Juliana M. Chan Chester L. Drum
author_sort	Siddharth Deshpande
title	Thermostable exoshells fold and stabilize recombinant proteins
title_short	Thermostable exoshells fold and stabilize recombinant proteins
title_full	Thermostable exoshells fold and stabilize recombinant proteins
title_fullStr	Thermostable exoshells fold and stabilize recombinant proteins
title_full_unstemmed	Thermostable exoshells fold and stabilize recombinant proteins
title_sort	thermostable exoshells fold and stabilize recombinant proteins
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/8a4348c6e72946be878fa93b29252878
work_keys_str_mv	AT siddharthdeshpande thermostableexoshellsfoldandstabilizerecombinantproteins AT nihardmasurkar thermostableexoshellsfoldandstabilizerecombinantproteins AT vallerinteavidemavelligirish thermostableexoshellsfoldandstabilizerecombinantproteins AT malandesai thermostableexoshellsfoldandstabilizerecombinantproteins AT goutamchakraborty thermostableexoshellsfoldandstabilizerecombinantproteins AT julianamchan thermostableexoshellsfoldandstabilizerecombinantproteins AT chesterldrum thermostableexoshellsfoldandstabilizerecombinantproteins
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Thermostable exoshells fold and stabilize recombinant proteins

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