Efficient protein production inspired by how spiders make silk

The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional...

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Autores principales:	Nina Kronqvist, Médoune Sarr, Anton Lindqvist, Kerstin Nordling, Martins Otikovs, Luca Venturi, Barbara Pioselli, Pasi Purhonen, Michael Landreh, Henrik Biverstål, Zigmantas Toleikis, Lisa Sjöberg, Carol V. Robinson, Nicola Pelizzi, Hans Jörnvall, Hans Hebert, Kristaps Jaudzems, Tore Curstedt, Anna Rising, Jan Johansson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6e88916356bd45a19c0f201d1ebfd6e8
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spelling	oai:doaj.org-article:6e88916356bd45a19c0f201d1ebfd6e82021-12-02T17:01:25ZEfficient protein production inspired by how spiders make silk10.1038/ncomms155042041-1723https://doaj.org/article/6e88916356bd45a19c0f201d1ebfd6e82017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15504https://doaj.org/toc/2041-1723The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.Nina KronqvistMédoune SarrAnton LindqvistKerstin NordlingMartins OtikovsLuca VenturiBarbara PioselliPasi PurhonenMichael LandrehHenrik BiverstålZigmantas ToleikisLisa SjöbergCarol V. RobinsonNicola PelizziHans JörnvallHans HebertKristaps JaudzemsTore CurstedtAnna RisingJan JohanssonNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nina Kronqvist Médoune Sarr Anton Lindqvist Kerstin Nordling Martins Otikovs Luca Venturi Barbara Pioselli Pasi Purhonen Michael Landreh Henrik Biverstål Zigmantas Toleikis Lisa Sjöberg Carol V. Robinson Nicola Pelizzi Hans Jörnvall Hans Hebert Kristaps Jaudzems Tore Curstedt Anna Rising Jan Johansson Efficient protein production inspired by how spiders make silk
description	The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.
format	article
author	Nina Kronqvist Médoune Sarr Anton Lindqvist Kerstin Nordling Martins Otikovs Luca Venturi Barbara Pioselli Pasi Purhonen Michael Landreh Henrik Biverstål Zigmantas Toleikis Lisa Sjöberg Carol V. Robinson Nicola Pelizzi Hans Jörnvall Hans Hebert Kristaps Jaudzems Tore Curstedt Anna Rising Jan Johansson
author_facet	Nina Kronqvist Médoune Sarr Anton Lindqvist Kerstin Nordling Martins Otikovs Luca Venturi Barbara Pioselli Pasi Purhonen Michael Landreh Henrik Biverstål Zigmantas Toleikis Lisa Sjöberg Carol V. Robinson Nicola Pelizzi Hans Jörnvall Hans Hebert Kristaps Jaudzems Tore Curstedt Anna Rising Jan Johansson
author_sort	Nina Kronqvist
title	Efficient protein production inspired by how spiders make silk
title_short	Efficient protein production inspired by how spiders make silk
title_full	Efficient protein production inspired by how spiders make silk
title_fullStr	Efficient protein production inspired by how spiders make silk
title_full_unstemmed	Efficient protein production inspired by how spiders make silk
title_sort	efficient protein production inspired by how spiders make silk
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6e88916356bd45a19c0f201d1ebfd6e8
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Efficient protein production inspired by how spiders make silk

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