Tuning the conformation and mechanical properties of silk fibroin hydrogels - ScienceDirect
Polymers | Free Full-Text | Microstructure Transitions and Dry-Wet Spinnability of Silk Fibroin Protein from Waste Silk Quilt
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![PDF] Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/daa6b91a8a661077da1f12c2de436e945172c41e/17-Figure1-1.png "PDF] Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils. | Semantic Scholar")
PDF] Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils. | Semantic Scholar
BETA SILK BLOUSE - Lurelly
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Atomistic model of spider silk nanostructure paves way for new class of synthetic materials
Molecules | Free Full-Text | Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) -Type II β-Turn, Not α-Helix-
Nanoconfinement controls stiffness, strength and mechanical toughness of β-sheet crystals in silk | Nature Materials
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BETA SILK BLOUSE - Lurelly
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Spider-silk inspired polymeric networks by harnessing the mechanical potential of β-sheets through network guided assembly | Nature Communications
Carbonization of a stable β-sheet-rich silk protein into a pseudographitic pyroprotein | Nature Communications
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Optimal Protein Sequence Design Mitigates Mechanical Failure in Silk β-Sheet Nanocrystals | ACS Biomaterials Science & Engineering
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On the strength of β-sheet crystallites of Bombyx mori silk fibroin | Journal of The Royal Society Interface
Dissecting the structural determinants for the difference in mechanical stability of silk and amyloid beta-sheet stacks - Physical Chemistry Chemical Physics (RSC Publishing) DOI:10.1039/C3CP00067B
Optimal Protein Sequence Design Mitigates Mechanical Failure in Silk β-Sheet Nanocrystals | ACS Biomaterials Science & Engineering
