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Biomolecular NMR Assignments

, Volume 10, Issue 1, pp 199–202 | Cite as

Resonance assignment of an engineered amino-terminal domain of a major ampullate spider silk with neutralized charge cluster

  • Daniel SchaalEmail author
  • Joschka Bauer
  • Kristian Schweimer
  • Thomas Scheibel
  • Paul Rösch
  • Stephan Schwarzinger
Article

Abstract

Spider dragline fibers are predominantly made out of the major ampullate spidroins (MaSp) 1 and 2. The assembly of dissolved spidroin into a stable fiber is highly controlled for example by dimerization of its amino-terminal domain (NRN) upon acidification, as well as removal of sodium chloride along the spinning duct. Clustered residues D39, E76 and E81 are the most highly conserved residues of the five-helix bundle, and they are hypothesized to be key residues for switching between a monomeric and a dimeric conformation. Simultaneous replacement of these residues by their non-titratable analogues results in variant D39N/E76Q/E81Q, which is supposed to fold into an intermediate conformation between that of the monomeric and the dimeric state at neutral pH. Here we report the resonance assignment of Latrodectus hesperus NRN variant D39N/E76Q/E81Q at pH 7.2 obtained by high-resolution triple resonance NMR spectroscopy.

Keywords

Spider silk Amino-terminal domain Major ampullate spidroin 1 Dimerization Latrodectus hesperus Acidic charge cluster 

Notes

Acknowledgments

Funding was obtained from the Deutsche Forschungsgemeinschaft DFG (SFB 840).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical standards

The authors declare that the experiments in this study comply with the current laws of the country in which they were performed.

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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  • Daniel Schaal
    • 2
    • 3
    Email author
  • Joschka Bauer
    • 1
  • Kristian Schweimer
    • 2
    • 3
  • Thomas Scheibel
    • 1
    • 3
    • 4
    • 5
    • 6
  • Paul Rösch
    • 2
    • 3
  • Stephan Schwarzinger
    • 2
    • 3
  1. 1.Lehrstuhl BiomaterialienUniversität BayreuthBayreuthGermany
  2. 2.Lehrstuhl BiopolymereUniversität BayreuthBayreuthGermany
  3. 3.Forschungszentrum für Bio-Makromoleküle (BIOmac)Universität BayreuthBayreuthGermany
  4. 4.Bayreuther Zentrum für Kolloide und Grenzflächen (BZKG)Universität BayreuthBayreuthGermany
  5. 5.Bayreuther Materialzentrum (BayMat)Universität BayreuthBayreuthGermany
  6. 6.Bayreuther Zentrum für Molekulare Biowissenschaften (BZMB)Universität BayreuthBayreuthGermany

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