Friedrich-Weygand Award 2011: The young investigator award in peptide and protein chemistry was assigned to Dr. Franz Hagn on occasion of the annual meeting of the Max Bergmann Society in Kloster Irsee, October 9–12, 2011. This review covers his lecture on that occasion.
A structural view on spider silk proteins and their role in fiber assembly
Article first published online: 8 MAY 2012
Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Volume 18, Issue 6, pages 357–365, June 2012
How to Cite
Hagn, F. (2012), A structural view on spider silk proteins and their role in fiber assembly. J. Peptide Sci., 18: 357–365. doi: 10.1002/psc.2417
- Issue published online: 18 MAY 2012
- Article first published online: 8 MAY 2012
- Manuscript Accepted: 19 APR 2012
- Manuscript Revised: 18 APR 2012
- Manuscript Received: 8 APR 2012
- NMR spectroscopy;
- spider silk;
Spider silk is the toughest known biomaterial and even outrivals modern synthetic high-performance materials. The question of understanding fiber formation is how the spider can prevent premature and fatal aggregation processes inside its own body and how the chemical and mechanical stimuli used to induce the fiber formation process translate into structural changes of the silk material, finally leading to controlled and irreversible aggregation. Here, the focus will be on the structure and function of the highly conserved N-domains and C-terminal domains of spider dragline silk which, unlike the very long repetitive sequence elements, adopt a folded conformation in solution and are therefore able to control intermolecular interactions and aggregation between other spider silk molecules. The structures of these domains add valuable details for the construction of a molecular picture of the complicated and highly optimized silk assembly process that might be beneficial for large-scale in vitro fiber formation attempts with recombinant silk material. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.