- Abstract:
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Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 2.4MB)
-
- Publisher copy:
- 10.1038/ncomms15504
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- Publisher:
- Nature Publishing Group Publisher's website
- Journal:
- Nature Communications Journal website
- Volume:
- 8
- Pages:
- 15504
- Publication date:
- 2017-05-05
- Acceptance date:
- 2017-04-04
- DOI:
- EISSN:
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2041-1723
- Pubs id:
-
pubs:698051
- URN:
-
uri:44fdc9c9-aab8-41a4-add6-07ae7be2a9cf
- UUID:
-
uuid:44fdc9c9-aab8-41a4-add6-07ae7be2a9cf
- Local pid:
- pubs:698051
- Language:
- English
- Keywords:
- Copyright holder:
- Robinson et al
- Copyright date:
- 2017
- Notes:
- © The Author(s) 2017. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Journal article
Efficient protein production inspired by how spiders make silk.
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Funding
Swedish Research Council
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FORMAS
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Vinnova
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Latvian Institute of Organic Synthesis
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