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| Andrea Nova; Sinan Keten; Nicola Pugno; Alberto Redaelli; Markus J. Buehler. |
| Spider silk is one of the strongest, most extensible and toughest biological materials known, exceeding the properties of many engineered materials including steel. Silks feature a hierarchical architecture where highly organized, densely H-bonded beta-sheet nanocrystals are arranged within a semi-amorphous protein matrix consisting of 31-helices and beta-turn protein structures. By using a bottom-up molecular-based mesoscale model that bridges the scales from Angstroms to hundreds of nanometers, here we show that the specific combination of a crystalline phase and a semi-amorphous matrix is crucial for the unique properties of silks. Specifically, our results reveal that the superior mechanical properties of spider silk can be explained solely by... |
| Tipo: Manuscript |
Palavras-chave: Chemistry; Bioinformatics; Earth & Environment. |
| Ano: 2010 |
URL: http://precedings.nature.com/documents/4336/version/1 |
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| Tristan Giesa; Melis Arslan; Nicola Pugno; Markus J. Buehler. |
| Silk is an exceptionally strong, extensible and tough material made from simple protein building blocks. The molecular structure of dragline spider silk repeat units consists of semi-amorphous and nanocrystalline beta-sheet protein domains. Here we show by a series of computational experiments how the nanoscale properties of silk repeat units are scaled up to create macroscopic silk fibers with outstanding mechanical properties despite the presence of cavities, tears and cracks. We demonstrate that the geometric confinement of silk fibrils to diameters of 50±30 nm width is critical to facilitate a powerful mechanism by which hundreds of thousands of protein domains synergistically resist deformation and failure to provide enhanced strength,... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Bioinformatics; Earth & Environment. |
| Ano: 2011 |
URL: http://precedings.nature.com/documents/5916/version/2 |
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