Conformational polymorphism, stability and aggregation in spider dragline silk proteins
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 polari...
| 主要な著者: | , , , |
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| フォーマット: | Journal article |
| 言語: | English |
| 出版事項: |
Elsevier
2005
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| 主題: |
| 要約: | 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. |
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