at Google ScholarTitle data
Hümmerich, Daniel ; Helsen, Christopher W. ; Quedzuweit, Susanne ; Oschmann, Jan ; Rudolph, Rainer ; Scheibel, Thomas:
Primary Structure Elements of Spider Dragline Silks and Their Contribution to Protein Solubility.
In: Biochemistry.
Vol. 43
(2004)
Issue 42
.
- pp. 13604-13612.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi048983q
Abstract in another language
Spider silk proteins have mainly been investigated with regard to their contribution to mechanical properties of the silk thread. However, little is known about the molecular mechanisms of silk assembly. As a first step toward characterizing this process, we aimed to identify primary structure elements of the garden spider's (Araneus diadematus) major dragline silk proteins ADF-3 and ADF-4 that determine protein solubility. In addition, we investigated the influence of conditions involved in mediating natural thread assembly on protein aggregation. Genes encoding spider silk-like proteins were generated using a cloning strategy, which is based on a combination of synthetic DNA modules and PCR-amplified authentic gene sequences. Comparing secondary structure, solubility, and aggregation properties of the synthesized proteins revealed that single primary structure elements have diverse influences on protein characteristics. Repetitive regions representing the largest part of dragline silk proteins determined the solubility of the synthetic proteins, which differed greatly between constructs derived from ADF-3 and ADF-4. Factors, such as acidification and increases in phosphate concentration, which promote silk assembly in vivo generally decreased silk protein solubility in vitro. Strikingly, this effect was pronounced in engineered proteins comprising the carboxyl-terminal nonrepetitive regions of ADF-3 or ADF-4, indicating that these regions might play an important role in initiating assembly of spider silk proteins.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| 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: | 29 Sep 2015 08:17 |
| Last Modified: | 20 Apr 2022 11:47 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/19783 |