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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Vollrath F,Hawkins N,Porter D,Holland C,Boulet-Audet Mdoi
10.1038/srep05625subject
Has Abstractpub_date
2014-07-09 00:00:00pages
5625issn
2045-2322pii
srep05625journal_volume
4pub_type
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