- Abstract:
-
Spider silk is spun in a complex and unique process, thought to depend on a hydriphobic conversion of a predominantly disordered to a β-sheet rich protein structures. To test this hypothesis we monitored the effect of cationic (DOTAC) and anionic (alkyl sulfate) detergents and of (ii) solvent polarity using a series of alcohols on the secondary structure transition in dilute solutions of native spidroin. Our results showed that the detergents hydrophilic head charge and hydrophobic tail lengt...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1016/j.ijbiomac.2005.06.004
-
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- Publisher:
- Elsevier Publisher's website
- Journal:
- International Journal of Biological Macromolecules Journal website
- Volume:
- 36
- Issue:
- 4
- Pages:
- 215-224
- Publication date:
- 2005-09-05
- DOI:
- ISSN:
-
0141-8130
- URN:
-
uuid:06dd48c1-20cb-4c5b-a35c-b1f72e71dcd1
- Local pid:
- ora:4207
- Language:
- English
- Keywords:
- Subjects:
- Copyright holder:
- Elsevier B. V.
- Copyright date:
- 2005
- Notes:
- The full-text of this article is not currently available in ORA, but you may be able to access the article via the publisher copy link on this record page.
Journal article
Conformational polymorphism, stability and aggregation in spider dragline silk proteins
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British Biological and Engineering Research Councils
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European Commission
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Danish Natural Sciences Research Council
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