Spider silk

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|'''''Spider Silk'''''
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|Spider silk is comparable in strength to carbon fibres
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|Highly structured at the nanometre scale – not good for synthetic materials
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|Repetitive structures- GXG motif
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|Glycine rich segments – hard and soft segments alternating
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| '''Hard'''= hydrogen bonding cross-linked crystallites (polyalanine) forming an amorphic beta sheet structure,
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|'''Soft'''= flexibility (Glycine rich)
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|Major protein from ''Nephila clavipes'' – MaSP1 tandem variants of
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|A GQG GYG GLG SQG A GRG GLG GQG A GA6GGx
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|MaSP2 also has a repetitive structure – difference soft segment contains proline containing pentamers: The consensus repeat is _GPGGY GPGQQ.3GPSGPGS A8.  Similar structure to Elastin – elastic properties of drag-line by the folding of pentamer structure.
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|In the spider – silk in 3 phases
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|1) Extremely viscous (withstand shear forces inside spider),
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|2) Liquid crystallite lower viscosity (near exit duct/glycine rich may be involved),
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|3) Insoluble fibre (result of dehydration and drawing).
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|'''MaSP1 and MaSP2''' – Drag line
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|'''MaSP1'''-Auxilary
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|'''MaSP2'''- Glue silk only
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|'''Neither'''- Cocoon silk
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|Super contraction associated with pentamer motif when wet: low visco-elasticity
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|Mimic natural proteins or simplify – Mimic structural significance still uncertain for some sequences
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|DPB1- Optimised for ''B.subtilis''
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|''B.subtilis'' potential host as simple secretion system compared to yeast. Secretion has advantages over expression in ''E.coli'' however; insufficient proportion of protein was secreted by yeast.
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| '''Fahnestock, S. R., Yao, Z., & Bedzyk, L. a. (2000). Microbial production of spider silk proteins. Journal of biotechnology, 74(2), 105-19. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11763501.'''
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Latest revision as of 10:38, 31 May 2010