Journal article
Structural diversity of native major ampullate, minor ampullate, cylindriform, and flagelliform silk proteins in solution
- Abstract:
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The foundations of silk spinning, the structure, storage, and activation of silk proteins, remain highly debated. By combining solution small-angle neutron and X-ray scattering (SANS and SAXS) alongside circular dichroism (CD), we reveal a shape anisotropy of the four principal native spider silk feedstocks from Nephila edulis. We show that these proteins behave in solution like elongated semiflexible polymers with locally rigid sections. We demonstrated that minor ampullate and cylindriform ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, 2.5MB, Terms of use)
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- Publisher copy:
- 10.1021/acs.biomac.0c00819
Authors
Bibliographic Details
- Publisher:
- American Chemical Society
- Journal:
- Biomacromolecules More from this journal
- Volume:
- 21
- Issue:
- 8
- Pages:
- 3387–3393
- Publication date:
- 2020-07-08
- Acceptance date:
- 2020-07-08
- DOI:
- EISSN:
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1526-4602
- ISSN:
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1525-7797
Item Description
- Language:
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English
- Keywords:
- Pubs id:
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1117072
- Local pid:
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pubs:1117072
- Deposit date:
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2020-07-08
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2020
- Rights statement:
- Copyright © 2020 American Chemical Society. This is an open access article published under CC BY 4.0.
- Licence:
- CC Attribution (CC BY)
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