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Differential Scanning Fluorimetry provides high throughput data on silk protein transitions

Abstract:
Here we present a set of measurements using Differential Scanning Fluorimetry (DSF) as an inexpensive, high throughput screening method to investigate the folding of silk protein molecules as they abandon their first native melt conformation, dehydrate and denature into their final solid filament conformation. Our first data and analyses comparing silks from spiders, mulberry and wild silkworms as well as reconstituted ‘silk’ fibroin show that DSF can provide valuable insights into details of silk denaturation processes that might be active during spinning. We conclude that this technique and technology offers a powerful and novel tool to analyse silk protein transitions in detail by allowing many changes to the silk solutions to be tested rapidly with microliter scale sample sizes. Such transition mechanisms will lead to important generic insights into the folding patterns not only of silks but also of other fibrous protein (bio)polymers
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/srep05625

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Institution:
University of Oxford
Role:
Author
ORCID:
0000-0003-3484-9005
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Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
ORCID:
0000-0003-0545-6771
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Institution:
University of Oxford
Role:
Author
ORCID:
0000-0003-0913-2221
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Institution:
University of Oxford
Role:
Author


Publisher:
Nature Research
Journal:
Scientific Reports More from this journal
Volume:
4
Issue:
1
Pages:
5625-5625
Publication date:
2014-07-09
DOI:
EISSN:
2045-2322
ISSN:
2045-2322


Language:
English
Keywords:
Pubs id:
475736
Local pid:
pubs:475736
Source identifiers:
W1990966214
Deposit date:
2026-03-04
ARK identifier:
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