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Conformational polymorphism, stability and aggregation in spider dragline silk proteins

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...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
"University of Oxford", "University of Aarhus, Denmark"
Department:
Institute for Storage Ring Facilities
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Mathematical,Physical & Life Sciences Division - Zoology
Role:
Author
More by this author
Institution:
"East Carolina University, NC, USA", "University of Aarhus, Denmark"
Department:
Institute for Storage Ring Facilities
Role:
Author
More by this author
Institution:
"University of Oxford", "University of Aarhus, Denmark"
Department:
Department of Zoology
Role:
Author
British Biological and Engineering Research Councils More from this funder
European Commission More from this funder
Danish Natural Sciences Research Council More from this funder
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

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