Title of article
Establishing the relationship between structure and mechanical function in silks
Author/Authors
Jelinski، نويسنده , , Lynn W، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1998
Pages
9
From page
237
To page
245
Abstract
Dragline silk protein fibers from the spider Nephila clavipes have mechanical properties that make them superior to high tenacity nylon, which is also a polyamide, and far superior to other protein fibers, including silkworm silk. In examining the relationship between the mechanical properties of the fibers and their molecular structure, one should look at the secondary structural elements, including β-sheets and bends, that have been derived by solid state NMR experiments and at the crystallinity and long-range structures obtained by X-ray measurements. A major conclusion from the present data is that nature has engineered in a certain amount of randomness, and that the protein is inadequately described as being simply a repeat of a consensus sequence. This suggests that approaches to designing synthetic silk-like proteins will need to include this randomness, rather than being based on high polymers of simple repeats of the consensus sequence.
Journal title
Current Opinion in Solid State and Materials Science
Serial Year
1998
Journal title
Current Opinion in Solid State and Materials Science
Record number
2088385
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