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

Eisoldt, Lukas and Hardy, John G. and Heim, Markus and Scheibel, Thomas R. (2010) The role of salt and shear on the storage and assembly of spider silk proteins. Journal of Structural Biology, 170 (2). pp. 413-419. ISSN 1047-8477

Full text not available from this repository.

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.

Item Type:
Journal Article
Journal or Publication Title:
Journal of Structural Biology
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1300/1315
Subjects:
ID Code:
75380
Deposited By:
Deposited On:
09 Sep 2015 06:32
Refereed?:
Yes
Published?:
Published
Last Modified:
07 Jan 2020 04:16