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Journal article

Efficient protein production inspired by how spiders make silk.

Abstract:

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...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1038/ncomms15504

Authors


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Swedish Research Council More from this funder
Latvian Institute of Organic Synthesis More from this funder
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:
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:

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