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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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| 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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| Raffaella Paparcone; Markus J. Buehler. |
| Amyloid fibrils and plaques are detected in the brain tissue of patients affected by Alzheimer’s disease, but have also been found as part of normal physiological processes such as bacterial adhesion. Due to their highly organized structures, amyloid proteins have also been used for the development of novel nanomaterials, for a variety of applications including biomaterials for tissue engineering, nanolectronics, or optical devices. Past research on amyloid fibrils resulted in advances in identifying their mechanical properties, revealing a remarkable stiffness. However, the failure mechanism under tensile loading has not been elucidated yet, despite its importance for the understanding of key mechanical properties of amyloid fibrils and plaques... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Neuroscience; Bioinformatics. |
| Ano: 2010 |
URL: http://precedings.nature.com/documents/5174/version/1 |
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