Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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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 -