Journal article
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 length cooperatively induced either a transition to the β-sheet rich form or a stable helical state. Changing the solvent polarity showed that HFIP and TFE induced formation of stable helical forms whereas MeOH, EtOH and IsoP induced a kinetically driven formulation of β-sheet rich structure.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Publisher copy:
- 10.1016/j.ijbiomac.2005.06.004
Authors
- Publisher:
- Elsevier
- Journal:
- International Journal of Biological Macromolecules More from this journal
- Volume:
- 36
- Issue:
- 4
- Pages:
- 215-224
- Publication date:
- 2005-09-01
- DOI:
- ISSN:
-
0141-8130
- Language:
-
English
- Keywords:
- Subjects:
- UUID:
-
uuid:06dd48c1-20cb-4c5b-a35c-b1f72e71dcd1
- Local pid:
-
ora:4207
- Deposit date:
-
2010-09-22
- ARK identifier:
Terms of use
- 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.
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