The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Spider silk as archetypal protein elastomer
Abstract
We present an overview of the physical properties of spider silks, and introduce a model designed to study the energy absorbed by the material as it stretches before breaking. Of particular interest are the inter- and intramolecular hydrogen bonds as well as the role of water in modifying the material properties of silk. A solid understanding of this interaction is of paramount importance for any deeper insights into the mechanical properties of any biomaterial. Here we note that the typical biological material has evolved to function in the fully hydrated elastomeric state. We conclude that silk after its transformation from the hydrated feedstock to the dehydrated fibre state can in fact be analysed in great detail and interpreted as representative of a wide range of elastomeric proteins covering, inter alia, bone, keratins, elastin and collagen.
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Cites
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
Cited by
Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
Knowles, T. P., Fitzpatrick, A. W., Meehan, S., Mott, H. R., Vendruscolo, M., Dobson, C. M., & Welland, M. E. (2007) · Science · doi:10.1126/science.1150057 · Cited by 782
Polymeric materials based on silk proteins
Hardy, J. G., Römer, L. M., & Scheibel, T. R. (2008) · Polymer · doi:10.1016/j.polymer.2008.08.006 · Cited by 506
Nova, A., Keten, S., Pugno, N. M., Redaelli, A., & Buehler, M. J. (2010) · Nano Letters · doi:10.1021/nl101341w · Cited by 414
Uncovering the structure–function relationship in spider silk
Yarger, J. L., Cherry, B. R., & van der Vaart, A. (2018) · Nature Reviews Materials · doi:10.1038/natrevmats.2018.8 · Cited by 357
Decoding the secrets of spider silk
Eisoldt, L., Smith, A., & Scheibel, T. (2011) · Materials Today · doi:10.1016/s1369-7021(11)70057-8 · Cited by 342
Metadata
- Authors
- Vollrath, F., & Porter, D.
- Venue
- Soft Matter
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2006
- Volume
- 2
- Issue
- 5
- Pages
- 377
- ISSN
- 1744-683X (ISSN-L)
- 1744-6848
- OpenAlex
- W2097123977
- Cited by
- 268
- References
- 1
- FWCI
- 7.51
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
