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    Novel assembly properties of recombinant spider dragline silk proteins

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    NMR show the crystalline regions to consist of pleated �-sheets of polyalanine stretches that give strength to the thread [5, 6], and the predominant secondary struc-and Biochemistry ture of the amorphous matrix is the glycine-rich 31-helix, Technische Universität München providing elasticity [7]. Freshly secreted silk proteins are 85747 Garching stored at high concentrations [8] as a liquid crystalline Germany spinning dope [9, 10] that is altered by changes in ionic 2Department of Zoology composition, pH (from pH 6.9 to 6.3) [11, 12], and wate
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