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| Theodor Ackbarow; Markus J. Buehler. |
| Proteins constitute the elementary building blocks of a vast variety of biological materials such as cellular protein networks, spider silk or bone, where they create extremely robust, multi-functional materials by self-organization of structures over many length- and time scales, from nano to macro. Some of the structural features are commonly found in a many different tissues, that is, they are highly conserved. Examples of such universal building blocks include alpha-helices, beta-sheets or tropocollagen molecules. In contrast, other features are highly specific to tissue types, such as particular filament assemblies, beta-sheet nanocrystals in spider silk or tendon fascicles. These examples illustrate that the coexistence of universality and... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Ecology; Molecular Cell Biology. |
| Ano: 2007 |
URL: http://precedings.nature.com/documents/826/version/1 |
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| Melis Arslan; Markus J. Buehler. |
| Silk is an ancient but remarkably strong, extensible and tough material made from simple protein building blocks. Earlier work has shown that the particular molecular geometry of silk with a composite of semi-amorphous and nanocrystalline beta-sheet protein domains provides the structural basis for its characteristic softening-stiffening behavior and remarkable strength at the nanoscale. Yet, an open question remains as to how these nanoscale properties are upscaled so effectively to create strong, extensible and tough silk fibers. Here we discover that the geometric confinement of fibrils to ≈50-100 nm width and arranged in bundles to form larger-scale silk fibers, is the key to explaining the upscaling of the mechanical properties of silk from... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Bioinformatics; Earth & Environment. |
| Ano: 2011 |
URL: http://precedings.nature.com/documents/5916/version/1 |
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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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