Title data
Hagenau, Anja ; Scheidt, Holger A. ; Serpell, Louise ; Huster, Daniel ; Scheibel, Thomas:
Structural Analysis of Proteinaceous Components in Byssal Threads of the Mussel Mytilus galloprovincialis.
In: Macromolecular Bioscience.
Vol. 9
(2009)
Issue 2
.
- pp. 162-168.
ISSN 1616-5195
DOI: https://doi.org/10.1002/mabi.200800271
Abstract in another language
The mussel byssus is a unique holdfast structure employed by marine mussels to colonize diverse substrates. The byssus consists of extracellular threads with mainly proteinaceous components. Individual threads reveal high tensile strength at their distal end and high elasticity in their proximal portion. Our studies show that proteins of the distal part are oriented along the thread axis and are well-ordered with a high β-structural content. In contrast, proteins of the proximal part are less ordered and are not as well-oriented with primarily α-helical structure. The detected differences in the structural features of the proteins along a byssus thread are likely an important basis for its gradual mechanical properties.
Further data
Item Type: | Article in a journal |
---|---|
Refereed: | Yes |
Keywords: | collagen; fiber; proteins; protein structure; solid-state NMR |
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: | 23 Sep 2015 12:32 |
Last Modified: | 10 Oct 2023 11:30 |
URI: | https://eref.uni-bayreuth.de/id/eprint/19495 |