Journal article
Differential scanning calorimetry of native silk feedstock
- Abstract:
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Native silk proteins, extracted directly from the silk gland prior to spinning, offer access to a naturally hydrated protein that has undergone little to no processing. Combined with differential scanning calorimetry (DSC), it is possible to probe the thermal stability and hydration status of silk and thus investigate its denaturation and solidification, echoing that of the natural spinning process. It is found that native silk is stable between −10 °C and 55 °C, and both the high‐temperature...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Version of record, pdf, 1.8MB)
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(Version of record, pdf, 939.8KB)
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- Publisher copy:
- 10.1002/mabi.201800228
Authors
Funding
Bibliographic Details
- Publisher:
- Wiley Publisher's website
- Journal:
- Macromolecular Bioscience Journal website
- Volume:
- 19
- Issue:
- 3
- Article number:
- 1800228
- Publication date:
- 2018-11-09
- DOI:
- EISSN:
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1616-5195
- ISSN:
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1616-5187
- Pmid:
-
30411857
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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pubs:942435
- UUID:
-
uuid:86b44434-d9f3-41c6-a067-cbe644b6c9f5
- Local pid:
- pubs:942435
- Source identifiers:
-
942435
- Deposit date:
- 2018-11-28
Terms of use
- Copyright holder:
- Holland et al
- Copyright date:
- 2018
- Notes:
-
Copyright © 2018 The Authors. Published by WILEY‐VCH Verlag GmbH and Co. KGaA, Weinheim.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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