Beta-silks : enhancing and controlling aggregation
Dicko, Cedric LU
; Kenney, John M
and Vollrath, Fritz
(2006)
In Advances in Protein Chemistry
73.
p.17-53
- Abstract
It appears that fiber-forming proteins are not an exclusive group but that, with appropriate conditions, many proteins can potentially aggregate and form fibrils; though only certain proteins, for example, amyloids and silks, do so under normal physiological conditions. Even so, this suggests a ubiquitous aggregation mechanism in which the protein environment is at least as important as the sequence. An ideal model system in which forced and natural aggregation has been observed is silk. Silks have evolved specifically to readily form insoluble ordered structures with a wide range of structural functionality. The animal, be it silkworm or spider, will produce, store, and transport high molecular weight proteins in a complex environment... (More)
It appears that fiber-forming proteins are not an exclusive group but that, with appropriate conditions, many proteins can potentially aggregate and form fibrils; though only certain proteins, for example, amyloids and silks, do so under normal physiological conditions. Even so, this suggests a ubiquitous aggregation mechanism in which the protein environment is at least as important as the sequence. An ideal model system in which forced and natural aggregation has been observed is silk. Silks have evolved specifically to readily form insoluble ordered structures with a wide range of structural functionality. The animal, be it silkworm or spider, will produce, store, and transport high molecular weight proteins in a complex environment to eventually allow formation of silk fibers with a variety of mechanical properties. Here we review fiber formation and its prerequisites, and discuss the mechanism by which the animal facilitates and modulates silk assembly to achieve controlled protein aggregation.
(Less)
- author
- Dicko, Cedric
LU
; Kenney, John M
and Vollrath, Fritz
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- keywords
- Animals, Protein Folding, Protein Structure, Secondary, Silk/chemistry
- in
- Advances in Protein Chemistry
- volume
- 73
- pages
- 37 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:17190610
- scopus:33845724091
- ISSN
- 0065-3233
- DOI
- 10.1016/S0065-3233(06)73002-9
- language
- English
- LU publication?
- no
- id
- 3e8e1be8-5155-4623-9818-05dcb036a342
- date added to LUP
- 2019-06-28 00:29:08
- date last changed
- 2024-01-01 13:51:24
@article{3e8e1be8-5155-4623-9818-05dcb036a342,
abstract = {{<p>It appears that fiber-forming proteins are not an exclusive group but that, with appropriate conditions, many proteins can potentially aggregate and form fibrils; though only certain proteins, for example, amyloids and silks, do so under normal physiological conditions. Even so, this suggests a ubiquitous aggregation mechanism in which the protein environment is at least as important as the sequence. An ideal model system in which forced and natural aggregation has been observed is silk. Silks have evolved specifically to readily form insoluble ordered structures with a wide range of structural functionality. The animal, be it silkworm or spider, will produce, store, and transport high molecular weight proteins in a complex environment to eventually allow formation of silk fibers with a variety of mechanical properties. Here we review fiber formation and its prerequisites, and discuss the mechanism by which the animal facilitates and modulates silk assembly to achieve controlled protein aggregation.</p>}},
author = {{Dicko, Cedric and Kenney, John M and Vollrath, Fritz}},
issn = {{0065-3233}},
keywords = {{Animals; Protein Folding; Protein Structure, Secondary; Silk/chemistry}},
language = {{eng}},
pages = {{17--53}},
publisher = {{Elsevier}},
series = {{Advances in Protein Chemistry}},
title = {{Beta-silks : enhancing and controlling aggregation}},
url = {{http://dx.doi.org/10.1016/S0065-3233(06)73002-9}},
doi = {{10.1016/S0065-3233(06)73002-9}},
volume = {{73}},
year = {{2006}},
}