at Google ScholarTitle data
Slotta, Ute ; Hess, Simone ; Spieß, Kristina ; Stromer, Thusnelda ; Serpell, Louise ; Scheibel, Thomas:
Spider Silk and Amyloid Fibrils : A Structural Comparison.
In: Macromolecular Bioscience.
Vol. 7
(2007)
Issue 2
.
- pp. 183-188.
ISSN 1616-5195
DOI: https://doi.org/10.1002/mabi.200600201
Abstract in another language
Although spider silks have been studied for decades, the assembly properties of the underlying silk proteins have still not been unravelled. Previously, the detection of amyloid-like nanofibrils in the spider's silk gland suggested their involvement in the assembly process.
Recombinantly produced spider silk also self-assembles into nanofibrils. In order to investigate the structural properties of such silk nanofibrils in more detail, they have been compared to amyloid-like fibrils to highlight structural similarities.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Keywords: | ADF-4; FT-IR; Sup35p; X-ray; yeast prion |
| 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 > Advanced Fields > Advanced Materials Profile Fields > Advanced Fields > Molecular Biosciences Profile Fields > Advanced Fields > Polymer and Colloid Science Profile Fields > Emerging Fields > Food and Health Sciences Profile Fields Profile Fields > Advanced Fields Profile Fields > Emerging Fields |
| Result of work at the UBT: | Yes |
| DDC Subjects: | 600 Technology, medicine, applied sciences 600 Technology, medicine, applied sciences > 620 Engineering |
| Date Deposited: | 25 Sep 2015 05:32 |
| Last Modified: | 10 Oct 2023 11:31 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/19545 |