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Differential scanning calorimetry of native silk feedstock

Abstract:

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
Version:
Publisher's Version

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Publisher copy:
10.1002/mabi.201800228

Authors


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Role:
Author
ORCID:
0000-0003-0913-2221
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Zoology
Role:
Author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Zoology
Role:
Author
ORCID:
0000-0003-0022-6934
More by this author
Role:
Author
ORCID:
0000-0001-8608-875X
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Zoology
Role:
Author
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Publisher:
Wiley Publisher's website
Journal:
Macromolecular Bioscience Journal website
Volume:
19
Issue:
3
Pages:
Article: 1800228
Publication date:
2018-11-09
DOI:
EISSN:
1616-5195
ISSN:
1616-5187
Pubs id:
pubs:942435
URN:
uri:86b44434-d9f3-41c6-a067-cbe644b6c9f5
UUID:
uuid:86b44434-d9f3-41c6-a067-cbe644b6c9f5
Local pid:
pubs:942435

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