Conformational polymorphism, stability and aggregation in spider dragline silks proteins
Dicko, Cedric LU
; Knight, David
; Kenney, John M.
and Vollrath, Fritz
(2005)
In International Journal of Biological Macromolecules
36(4).
p.215-224
- Abstract
Spider silk is spun in a complex and unique process, thought to depend on a hydrophobic 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... (More)
Spider silk is spun in a complex and unique process, thought to depend on a hydrophobic 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 formation of β-sheet rich structure.
(Less)
- author
- Dicko, Cedric
LU
; Knight, David
; Kenney, John M.
and Vollrath, Fritz
- publishing date
- 2005-09-15
- type
- Contribution to journal
- publication status
- published
- keywords
- Conformational stability, Hydrophobic interactions, Silk aggregation
- in
- International Journal of Biological Macromolecules
- volume
- 36
- issue
- 4
- pages
- 10 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:23944509056
- pmid:16102807
- ISSN
- 0141-8130
- DOI
- 10.1016/j.ijbiomac.2005.06.004
- language
- English
- LU publication?
- no
- id
- f9aa627e-52ea-44b4-9ec7-18bf8b01015d
- date added to LUP
- 2019-06-28 00:23:40
- date last changed
- 2024-04-30 15:46:01
@article{f9aa627e-52ea-44b4-9ec7-18bf8b01015d,
abstract = {{<p>Spider silk is spun in a complex and unique process, thought to depend on a hydrophobic 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 formation of β-sheet rich structure.</p>}},
author = {{Dicko, Cedric and Knight, David and Kenney, John M. and Vollrath, Fritz}},
issn = {{0141-8130}},
keywords = {{Conformational stability; Hydrophobic interactions; Silk aggregation}},
language = {{eng}},
month = {{09}},
number = {{4}},
pages = {{215--224}},
publisher = {{Elsevier}},
series = {{International Journal of Biological Macromolecules}},
title = {{Conformational polymorphism, stability and aggregation in spider dragline silks proteins}},
url = {{http://dx.doi.org/10.1016/j.ijbiomac.2005.06.004}},
doi = {{10.1016/j.ijbiomac.2005.06.004}},
volume = {{36}},
year = {{2005}},
}