Spider silks structures

Romer, L. and Scheibel, T. 2008. The elaborate structure of spider silk Structure and function of a natural high performance fiber. Prion, 2,154-61. 

The complexity and versatility of materials made by nature are the envy of scientists. We are only beginning to be able to create materials that have the strong yet porous structure of bone or the strength and flexibility of spider silk (Section 19.13). However, some materials are not strong they are soft and flexible. These materials, some of which are described in the following two sections, are also important to industry and medicine and some are vital to life. 

The structures of some natural protein-based materials, such as silk and wool, result in strong, tough fibers. Spiders and silkworms use proteins as a structural material of remarkable strength (Fig. 19.22). Chemists are duplicating nature by making artificial spider silk (Fig. 19.23), which is one of the strongest fibers known. 

Hayash C.I., Shipley N., and Lewis R., Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins, Int. J. Biol. Macromol., 24, 271, 1999. 

Parkhe AD, Seeley SK, Gardner K (1997) Structural studies of spider silk proteins in the fiber. J Mol Recognit 10 1-6... 

Slotta U, Hess S, Spiess K et al (2007) Spider silk and amyloid fibrils a structural comparison. Macromol Biosci 7 183-188... 

Fig. 4. Time-induced conformational change of spider silk protein (spidroin) in solution. Solutions of silk proteins at 1% w/v in distilled water were monitored using circular dichroism. The graph shows a change in secondary structure with time. The silk proteins underwent a kinetically driven transition from a partially unfolded structure to a -sheet-rich structure (from Dicko et al., 2004c). ( ) after 0 days, (O) after 1 day, and (A) after 2 days. The conformational change appeared faster at 20°C compared to 5°C, suggesting a hydrophobically driven mechanism. (Copyright 2004 American Chemical Society.)...

Frische, S., Maunsbach, A. B., and Vollrath, F. (1998). Elongate cavities and skin-core structure in Nephila spider silk observed by electron microscopy. Journal of Microscopy 189, 64-70. 

Hayashi, C. Y., and Lewis, R. V. (1998). Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks. J. Mol. Biol. 275, 773-784. 

Rossle, M., Panine, P., Urban, V. S., and Riekel, C. (2004). Structural evolution of regenerated silk fibroin under shear Combined wide- and small-angle x-ray scattering experiments using synchrotron radiation. Biopolymers 74, 316-327. Rousseau, M. E., Lefevre, T., Beaulieu, L., Asakura, T., and Pezolet, M. (2004). Study of protein conformation and orientation in silkworm and spider silk fibres using Raman microspectroscopy. Biomacromolecules 5, 2247-2257. 

Vollrath, F. (2000b). Strength and structure of spiders silks. Rev. Mol. Biotechnol. 74, 67-83. 

Although much of the interest in biological nanostructures has focused on relatively complex functionality, cells and organisms themselves can be considered as a collection of self-assembled materials lipid bilayers, the extracellular matrix, tendon and connective tissue, skin, spider silk, cotton fiber, wood, and bone are all self-assembled biological materials, with an internal structure hierarchically ordered from the molecular to the macroscopic scale. 

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