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| Alfonso Gautieri; Simone Vesentini; Alberto Redaelli; Markus J. Buehler. |
| Collagen constitutes one third of the human proteome, providing mechanical stability, elasticity and strength to organisms and is thus the prime construction materials in biology. Collagen is also the dominating material in the extracellular matrix and its stiffness controls cell differentiation, growth and pathology. However, the origin of the unique mechanical properties of collagenous tissues, and in particular its stiffness, extensibility and nonlinear mechanical response remains unknown. By using x-ray diffraction data of a collagen fibril (Orgel et al., PNAS, 2006) here we present an experimentally validated model of the nanomechanics of a collagen microfibril that incorporates the full biochemical details of the amino acid sequence of constituting... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Bioinformatics. |
| Ano: 2010 |
URL: http://precedings.nature.com/documents/4995/version/2 |
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| Alfonso Gautieri; Simone Vesentini; Alberto Redaelli; Markus J. Buehler. |
| Collagen constitutes one third of the human proteome, providing mechanical stability, elasticity and strength to connective tissues. Collagen is also the dominating material in the extracellular matrix (ECM) and is thus crucial for cell differentiation, growth and pathology. However, fundamental questions remain with respect to the origin of the unique mechanical properties of collagenous tissues, and in particular its stiffness, extensibility and nonlinear mechanical response. By using x-ray diffraction data of a collagen fibril reported by Orgel et al. (Proceedings of the National Academy of Sciences USA, 2006) in combination with protein structure identification methods, here we present an experimentally validated model of the nanomechanics of a... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Bioinformatics. |
| Ano: 2010 |
URL: http://precedings.nature.com/documents/4995/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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