The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
The molecular structure of spider dragline silk: Folding and orientation of the protein backbone
Open accessAbstract
The design principles of spider dragline silk, nature's high-performance fiber, are still largely unknown, in particular for the noncrystalline glycine-rich domains, which form the bulk of the material. Here we apply two-dimensional solid-state NMR to determine the distribution of the backbone torsion angles (φ,ψ) as well as the orientation of the polypeptide backbone toward the fiber at both the glycine and alanine residues. Instead of an “amorphous matrix,” suggested earlier for the glycine-rich domains, these new data indicate that all domains in dragline silk have a preferred secondary structure and are strongly oriented, with the chains predominantly parallel to the fiber. As proposed previously, the alanine residues are predominantly found in a β sheet conformation. The glycine residues are partly incorporated into the β sheets and otherwise form helical structures with an approximate 3-fold symmetry.
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Citations
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Cited by
Altman, G. H., Diaz, F., Jakuba, C., Calabro, T., Horan, R. L., Chen, J., Lu, H., Richmond, J., & Kaplan, D. L. (2003) · Biomaterials · doi:10.1016/s0142-9612(02)00353-8 · Cited by 3,458
Mechanism of silk processing in insects and spiders
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The Biomedical Use of Silk: Past, Present, Future
Holland, C., Numata, K., Rnjak‐Kovacina, J., & Seib, F. P. (2019) · Advanced Healthcare Materials · doi:10.1002/adhm.201800465 · Cited by 815
Protein Secondary Structure and Orientation in Silk as Revealed by Raman Spectromicroscopy
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Metadata
- Authors
- van Beek, J. D., Hess, S., Vollrath, F., & Meier, B. H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-07-29
- Volume
- 99
- Issue
- 16
- Pages
- 10266-10271
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2167668845
- Cited by
- 502
- References
- 30
- FWCI
- 10.42
- Type
- journal article
- Language
- en
- Open access
- green
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