Schlagwort(e):
Biotechnology.
;
Electronic books.
Beschreibung / Inhaltsverzeichnis:
This book offers a snapshot of the current state of the art of research and development on the properties and characteristics of silk and their use in medicine and industry. It includes recent advances in research on both spider and insect silks.
Materialart:
Online-Ressource
Seiten:
1 online resource (277 pages)
Ausgabe:
1st ed.
ISBN:
9789400771192
Serie:
Biologically-Inspired Systems Series ; v.5
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=1538965
DDC:
677/.39
Sprache:
Englisch
Anmerkung:
Intro -- Preface -- Contents -- Chapter 1 Wild Silk Production to Support Farmers Excluded from Protected Areas in Madagascar -- 1.1 Introduction -- 1.2 Methodology -- 1.2.1 Techno-Economic Modeling -- 1.2.2 Modules and Submodules -- 1.3 Results -- 1.4 Discussion -- 1.4.1 Economic Potential -- 1.4.2 Environmental Potential -- 1.4.3 Enterprise Versus Payments for Ecosystem Services -- 1.5 Conclusions -- References -- Chapter 2 Evolutionary Divergence of Lepidopteran and Trichopteran Fibroins -- 2.1 Introduction -- 2.2 The Fibroins of Saturniidae (Wild Silkmoth) -- 2.3 Antheraea pernyi and Antheraea yamamai Fibroins -- 2.4 Differences Between the Fibroins of A. pernyi and A. yamamai -- 2.5 Structure Divergence and Conservation Found in the Fibroins of Antheraea myllita -- 2.6 Fibroins of Saturniidae Species Other than Antheraea -- 2.7 Three Components of Bombyx mori Silk Fiber Protein -- 2.8 The Bombyx fhc -- 2.9 Silk Fiber Proteins of Other Lepidopteran Species -- 2.10 Genetic Divergence Between Nonrepetitive Parts of fhc -- 2.11 Low Molecular-Weight Components of Bombyx Silk Filament -- 2.12 Fibroin Light Chain (flc) in Lepidoptera Other than Bombyx -- 2.13 P25 Proteins in Lepidoptera Other than Saturniidae -- 2.14 Silk Proteins of Three Diverse Trichopteran Species -- 2.15 Evolution of Fibroins -- References -- Chapter 3 The Silk I and Lamella Structures of (Ala-Gly)15 as the Model of Bombyx mori Silk Fibroin Studied with Solid State NMR -- 3.1 Introduction -- 3.2 Silk I Structure -- 3.3 Lamella Structure -- References -- Chapter 4 Application of Bombyx mori Silk Fibroin as a Biomaterial for Vascular Grafts -- 4.1 Introduction -- 4.2 Several Forms of Silk Fibroin for Biomaterial Applications -- 4.3 Application to Vascular Graft -- 4.4 Conclusion -- References -- Chapter 5 Evolution and Application of Coiled Coil Silks from Insects.
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5.1 Introduction -- 5.2 Function of Coiled Coil Materials -- 5.3 Molecular Structure of Proteins -- 5.3.1 X-Ray Diffraction Data -- 5.3.2 Solid-State NMR Data -- 5.3.3 Raman Data -- 5.4 The Coiled Coil Silk Proteins -- 5.4.1 Amino Acid Composition of Silk -- 5.4.2 Number and Architecture of the Proteins -- 5.4.3 Coiled Coil Core Composition -- 5.4.4 Cross-Linking Between Proteins -- 5.5 Accessory Proteins -- 5.6 Artificial Materials Based on Coiled Coil Silks -- 5.6.1 Artificial Materials from Recombinant Coiled Coil Silks -- 5.6.2 Artificial Materials from Natural Coiled Coil Silks -- 5.7 Conclusions -- References -- Chapter 6 Characterization of Underwater Silk Proteins from Caddisfly Larva, Stenopsyche marmorata -- 6.1 Introduction -- 6.2 Complete Purification of Larval Silk Proteins from the Stenopsychidae Caddisfly, Stenopsyche marmorata -- 6.3 Characteristics of the Smsp-1 Primary Structure I: O-Phosphorylation on Ser Residues -- 6.4 Characteristics of the Smsp-1 Primary Structure II: Amino Acid Composition -- 6.5 Characteristics of the Smsp-1 Primary Structure III: Long Range Periodic Amino Acid Sequence -- 6.6 Related Studies and Perspectives -- References -- Chapter 7 Atomic Force Microscopy and Spectroscopy of Silk from Spider Draglines, Capture-Web Spirals, and Silkworms -- 7.1 Introduction -- 7.2 Atomic Force Microscope (AFM) -- 7.3 AFM Imaging of Silks -- 7.3.1 Segmented Nanofibers -- 7.3.2 Silk Globules -- 7.3.3 Other AFM Imaging -- 7.4 Pulling and Pushing with the AFM Tip -- 7.4.1 AFM Pulling - Force Spectroscopy -- 7.4.2 Dragline Silk Proteins -- 7.4.3 Capture Silk -- 7.4.4 AFM Pushing - Nanoindentation -- 7.4.5 Force Mapping - Force-Volume Imaging -- 7.5 Concluding Remarks -- References -- Chapter 8 Modular Spider Silk Fibers: Defining New Modules and Optimizing Fiber Properties -- 8.1 Introduction -- 8.2 Cloning of the Piriform Silk.
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8.3 Changing Fiber Structure and Properties by Module Composition and by Post-spin Draw Modification -- 8.4 Conclusion -- References -- Chapter 9 How to Pass the Gap - Functional Morphology and Biomechanics of Spider Bridging Threads -- 9.1 Introduction -- 9.2 Materials and Methods -- 9.2.1 Behavioural Observations -- 9.2.2 Adhesion Measurements -- 9.2.3 Scanning Electron Microscopy (SEM) -- 9.3 Results -- 9.3.1 Bridging Behaviour and Success -- 9.3.2 Bridging Line and Dragline Adhesion -- 9.3.3 Thread Morphology -- 9.4 Discussion -- 9.4.1 Are Bridging Lines Adhesive? -- 9.4.2 The Role of Drag Forces and Friction in Bridging Line Adhesion -- 9.4.3 Structural Principles of Adhesive Silk Applications -- 9.4.4 The Role of Bridging in Colonization of Smooth Surfaces -- 9.5 Conclusions -- References -- Chapter 10 The Power of Recombinant Spider Silk Proteins -- 10.1 Introduction -- 10.2 Recombinant Production of Dragline Silk Proteins -- 10.3 Processing of Recombinant Spider Silk Proteins -- 10.3.1 Fibers -- 10.3.1.1 Wet Spinning -- 10.3.1.2 Biomimetic Spinning -- 10.3.2 Non-woven Meshes Made of Recombinant Spider Silk Proteins -- 10.4 Modification of Recombinant Silk Proteins -- 10.4.1 Genetic Engineering -- 10.4.1.1 Biomineralisation -- 10.4.1.2 Cell Adhesion -- 10.4.1.3 Gene Delivery -- 10.4.1.4 Antimicrobial Silk -- 10.4.1.5 Others -- 10.4.2 Chemical Functionalization -- 10.4.3 Silk-Polymer Hybrids -- 10.5 Outlook -- References -- Chapter 11 Prey Capture Adhesives Produced by Orb-Weaving Spiders -- 11.1 Introduction to Orb Webs -- 11.2 Cribellar Silk -- 11.3 Viscid Silk -- 11.4 Comparing Cribellar and Viscid Capture Silk -- 11.5 Summary/Conclusion -- References -- Chapter 12 Silk and Web Synergy: The Merging of Material and Structural Performance -- 12.1 Introduction: Biomimicry and Stealing Ideas from Silk -- 12.2 A Complex Biological Material.
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12.2.1 Molecular Structure and Mechanics of Silk -- 12.2.2 The "Model" Behavior of Silk -- 12.3 From Silk Threads to Spider Webs -- 12.3.1 Defects and Flaw Tolerance -- 12.3.2 Constitutive Behavior Comparison -- 12.3.3 Stability Under Global Loading -- 12.3.4 Damage Minimization and Fracture Mechanics -- 12.4 "Universal" Attachments -- 12.4.1 Theory of Multiple Peeling -- 12.4.2 Synergetic Optimization of Structure and Material -- 12.4.3 Hierarchical Branching: Smaller Is Stronger -- 12.4.4 Computational Validation of Attachments -- 12.4.5 Detachment Under Wind Loading -- 12.5 Conclusion -- References -- Index.
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