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Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects

Dicko, Cedric LU orcid ; Knight, David ; Kenney, John M. and Vollrath, Fritz (2004) In Biomacromolecules 5(6). p.2105-2115
Abstract

Orb weaver spiders use exceptionally complex spinning processes to transform soluble silk proteins into solid fibers with specific functions and mechanical properties. In this study, to understand the nature of this transformation we investigated the structural changes of the soluble silk proteins from the major ampullate gland (web radial threads and spider safety line); flagelliform gland (web sticky spiral threads); minor ampullate gland (web auxiliary spiral threads); and cylindrical gland (egg sac silk). Using circular dichroism, we elucidated (i) the different structures and folds for the various silk proteins; (ii) irreversible temperature-induced transitions of the various silk structures toward β-sheet-rich final states; and... (More)

Orb weaver spiders use exceptionally complex spinning processes to transform soluble silk proteins into solid fibers with specific functions and mechanical properties. In this study, to understand the nature of this transformation we investigated the structural changes of the soluble silk proteins from the major ampullate gland (web radial threads and spider safety line); flagelliform gland (web sticky spiral threads); minor ampullate gland (web auxiliary spiral threads); and cylindrical gland (egg sac silk). Using circular dichroism, we elucidated (i) the different structures and folds for the various silk proteins; (ii) irreversible temperature-induced transitions of the various silk structures toward β-sheet-rich final states; and (iii) the role of protein concentration in silk storage and transport. We discuss the implication of these results in the spinning process and a possible mechanism for temperature-induced β-sheet formation.

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author
; ; and
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomacromolecules
volume
5
issue
6
pages
11 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:9744257710
  • pmid:15530023
ISSN
1525-7797
DOI
10.1021/bm034486y
language
English
LU publication?
no
id
e65e51e1-c8fa-4a21-8883-c6147a2e4a51
date added to LUP
2019-06-28 00:24:05
date last changed
2024-05-28 18:52:03
@article{e65e51e1-c8fa-4a21-8883-c6147a2e4a51,
  abstract     = {{<p>Orb weaver spiders use exceptionally complex spinning processes to transform soluble silk proteins into solid fibers with specific functions and mechanical properties. In this study, to understand the nature of this transformation we investigated the structural changes of the soluble silk proteins from the major ampullate gland (web radial threads and spider safety line); flagelliform gland (web sticky spiral threads); minor ampullate gland (web auxiliary spiral threads); and cylindrical gland (egg sac silk). Using circular dichroism, we elucidated (i) the different structures and folds for the various silk proteins; (ii) irreversible temperature-induced transitions of the various silk structures toward β-sheet-rich final states; and (iii) the role of protein concentration in silk storage and transport. We discuss the implication of these results in the spinning process and a possible mechanism for temperature-induced β-sheet formation.</p>}},
  author       = {{Dicko, Cedric and Knight, David and Kenney, John M. and Vollrath, Fritz}},
  issn         = {{1525-7797}},
  language     = {{eng}},
  month        = {{11}},
  number       = {{6}},
  pages        = {{2105--2115}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biomacromolecules}},
  title        = {{Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects}},
  url          = {{http://dx.doi.org/10.1021/bm034486y}},
  doi          = {{10.1021/bm034486y}},
  volume       = {{5}},
  year         = {{2004}},
}