Please use this identifier to cite or link to this item: https://doi.org/10.1073/pnas.0813255106
DC FieldValue
dc.titleSolution structure of eggcase silk protein and its implications for silk fiber formation
dc.contributor.authorLin, Z.
dc.contributor.authorHuang, W.
dc.contributor.authorZhang, J.
dc.contributor.authorFan, J.-S.
dc.contributor.authorYang, D.
dc.date.accessioned2014-10-27T08:39:58Z
dc.date.available2014-10-27T08:39:58Z
dc.date.issued2009-06-02
dc.identifier.citationLin, Z., Huang, W., Zhang, J., Fan, J.-S., Yang, D. (2009-06-02). Solution structure of eggcase silk protein and its implications for silk fiber formation. Proceedings of the National Academy of Sciences of the United States of America 106 (22) : 8906-8911. ScholarBank@NUS Repository. https://doi.org/10.1073/pnas.0813255106
dc.identifier.issn00278424
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101694
dc.description.abstractSpider silks are renowned for their excellent mechanical properties and biomimetic and industrial potentials. They are formed from the natural refolding of water-soluble fibroins with α-helical and random coil structures in silk glands into insoluble fibers with mainly β-structures. The structures of the fibroins at atomic resolution and silk formation mechanism remain largely unknown. Here, we report the 3D structures of individual domains of a ≈366-kDa eggcase silk protein that consists of 20 identical type 1 repetitive domains, one type 2 repetitive domain, and conserved nonrepetitive N- and C-terminal domains. The structures of the individual domains in solution were determined by using NMR techniques. The domain interactions were investigated by NMR and dynamic light-scattering techniques. The formation of micelles and macroscopic fibers from the domains was examined by electron microscopy. We find that either of the terminal domains covalently linked with at least one repetitive domain spontaneously forms micelle-like structures and can be further transformed into fibers at ≥37°C and a protein concentration of >0.1 wt%. Our biophysical and biochemical experiments indicate that the less hydrophilic terminal domains initiate the assembly of the proteins and form the outer layer of the micelles whereas the more hydrophilic repetitive domains are embedded inside to ensure the formation of the micelle-like structures that are the essential intermediates in silk formation. Our results establish the roles of individual silk protein domains in fiber formation and provide the basis for designing miniature fibroins for producing artificial silks.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1073/pnas.0813255106
dc.sourceScopus
dc.subjectNMR
dc.subjectSpider silk
dc.subjectStructural transition
dc.subjectTuSp1
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1073/pnas.0813255106
dc.description.sourcetitleProceedings of the National Academy of Sciences of the United States of America
dc.description.volume106
dc.description.issue22
dc.description.page8906-8911
dc.description.codenPNASA
dc.identifier.isiut000266580500025
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

55
checked on Oct 16, 2019

WEB OF SCIENCETM
Citations

50
checked on Oct 16, 2019

Page view(s)

26
checked on Oct 12, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.