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Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
- Source :
- Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
- Publication Year :
- 2018
- Publisher :
- Nature Portfolio, 2018.
-
Abstract
- β-sheet structure underlies the mechanical properties of spider silk but the mechanism to form β-sheet from soluble silk protein during transition into insoluble fibers has not been elucidated. Here the authors unravel the mechanism of β-sheet formation using NMR and circular dichroism spectroscopy.
- Subjects :
- Science
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 9
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Nature Communications
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.7dec962a6e3241d294a8b3fa08fe5322
- Document Type :
- article
- Full Text :
- https://doi.org/10.1038/s41467-018-04570-5