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Acidic Residues Control the Dimerization of the N-terminal Domain of Black Widow Spiders’ Major Ampullate Spidroin 1

DOI zum Zitieren dieses Dokuments: https://doi.org/10.1038/srep34442

Title data

Bauer, Joschka ; Schaal, Daniel ; Eisoldt, Lukas ; Schweimer, Kristian ; Schwarzinger, Stephan ; Scheibel, Thomas:
Acidic Residues Control the Dimerization of the N-terminal Domain of Black Widow Spiders’ Major Ampullate Spidroin 1.
In: Scientific Reports. (29 September 2016) .
ISSN 2045-2322
DOI: https://doi.org/10.1038/srep34442

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Abstract

Dragline silk is the most prominent amongst spider silks and comprises two types of major ampullate spidroins (MaSp) differing in their proline content. In the natural spinning process, the conversion of soluble MaSp into a tough fiber is, amongst other factors, triggered by dimerization and conformational switching of their helical amino-terminal domains (NRN). Both processes are induced by protonation of acidic residues upon acidification along the spinning duct. Here, the structure and monomer-dimer-equilibrium of the domain NRN1 of Latrodectus hesperus MaSp1 and variants thereof have been investigated, and the key residues for both could be identified. Changes in ionic composition and strength within the spinning duct enable electrostatic interactions between the acidic and basic pole of two monomers which prearrange into an antiparallel dimer. Upon naturally occurring acidification this dimer is stabilized by protonation of residue E114. A conformational change is independently triggered by protonation of clustered acidic residues (D39, E76, E81). Such step-by-step mechanism allows a controlled spidroin assembly in a pH- and salt sensitive manner, preventing premature aggregation of spider silk proteins in the gland and at the same time ensuring fast and efficient dimer formation and stabilization on demand in the spinning duct.

Further data

Item Type: Article in a journal
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Emerging Fields
Profile Fields > Emerging Fields > Food and Health Sciences
Research Institutions
Research Institutions > Research Centres
Research Institutions > Research Centres > Bayreuth Center for Material Science and Engineering - BayMAT
Language: English
Originates at UBT: Yes
Date Deposited: 07 Oct 2016 08:42
Last Modified: 19 Apr 2018 10:32
URI: https://epub.uni-bayreuth.de/id/eprint/3653

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