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In replica-exchange MD structures of Nephila clavipes MaSp1 and MaSp2, poly-alanine regions predominantly form distinct, orderly beta-sheet crystal domains, while glycine-rich repeats form disordered regions of 3₁-helix-type structures and beta-turns.
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Sinan Keten et al., “Nanostructure and molecular mechanics of spider dragline silk protein assemblies”, Journal of The Royal Society Interface 7, 1709-1721 (2010), doi:10.1098/rsif.2010.0149; Abstract. Scope: MaSp1 and MaSp2 dragline silk proteins, Nephila clavipes, replica-exchange MD
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Sinan Keten, Markus J. Buehler. Nanostructure and molecular mechanics of spider dragline silk protein assemblies. Journal of The Royal Society Interface 7, 1709-1721 (2010). doi:10.1098/rsif.2010.0149
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Nanostructure and molecular mechanics of spider dragline silk protein assemblies
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The structural analysis reveals that poly-alanine regions in silk predominantly form distinct and orderly beta-sheet crystal domains, while disorderly regions are formed by glycine-rich repeats that consist of 3₁-helix type structures and beta-turns.
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Abstract of Nanostructure and molecular mechanics of spider dragline silk protein assemblies, as read
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