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The role of salt and shear on the storage and assembly of spider silk proteins

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The role of salt and shear on the storage and assembly of spider silk proteins. / Eisoldt, Lukas; Hardy, John G.; Heim, Markus; Scheibel, Thomas R.

In: Journal of Structural Biology, Vol. 170, No. 2, 05.2010, p. 413-419.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Eisoldt, L, Hardy, JG, Heim, M & Scheibel, TR 2010, 'The role of salt and shear on the storage and assembly of spider silk proteins', Journal of Structural Biology, vol. 170, no. 2, pp. 413-419. https://doi.org/10.1016/j.jsb.2009.12.027

APA

Eisoldt, L., Hardy, J. G., Heim, M., & Scheibel, T. R. (2010). The role of salt and shear on the storage and assembly of spider silk proteins. Journal of Structural Biology, 170(2), 413-419. https://doi.org/10.1016/j.jsb.2009.12.027

Vancouver

Eisoldt L, Hardy JG, Heim M, Scheibel TR. The role of salt and shear on the storage and assembly of spider silk proteins. Journal of Structural Biology. 2010 May;170(2):413-419. https://doi.org/10.1016/j.jsb.2009.12.027

Author

Eisoldt, Lukas ; Hardy, John G. ; Heim, Markus ; Scheibel, Thomas R. / The role of salt and shear on the storage and assembly of spider silk proteins. In: Journal of Structural Biology. 2010 ; Vol. 170, No. 2. pp. 413-419.

Bibtex

@article{132881b57bdc47859f7cec1ef2cd8348,
title = "The role of salt and shear on the storage and assembly of spider silk proteins",
abstract = "Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.",
keywords = "Spider silk, Protein assembly, Salt, Shear, MAJOR AMPULLATE GLAND, C-TERMINAL DOMAIN, FIBER FORMATION, HOFMEISTER SERIES, DRAGLINE, CONFORMATION, ORIENTATION, MECHANISM, INSECTS, FIBROIN, Biochemistry, Genetics and Molecular Biology(all), Biomaterials",
author = "Lukas Eisoldt and Hardy, {John G.} and Markus Heim and Scheibel, {Thomas R.}",
year = "2010",
month = may,
doi = "10.1016/j.jsb.2009.12.027",
language = "English",
volume = "170",
pages = "413--419",
journal = "Journal of Structural Biology",
issn = "1047-8477",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - The role of salt and shear on the storage and assembly of spider silk proteins

AU - Eisoldt, Lukas

AU - Hardy, John G.

AU - Heim, Markus

AU - Scheibel, Thomas R.

PY - 2010/5

Y1 - 2010/5

N2 - Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.

AB - Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.

KW - Spider silk

KW - Protein assembly

KW - Salt

KW - Shear

KW - MAJOR AMPULLATE GLAND

KW - C-TERMINAL DOMAIN

KW - FIBER FORMATION

KW - HOFMEISTER SERIES

KW - DRAGLINE

KW - CONFORMATION

KW - ORIENTATION

KW - MECHANISM

KW - INSECTS

KW - FIBROIN

KW - Biochemistry, Genetics and Molecular Biology(all)

KW - Biomaterials

U2 - 10.1016/j.jsb.2009.12.027

DO - 10.1016/j.jsb.2009.12.027

M3 - Journal article

VL - 170

SP - 413

EP - 419

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

IS - 2

ER -