Methionine Redox Controlled Crystallization of Biosynthetic Silk Spidroin
Methionine Redox Controlled Crystallization of Biosynthetic Silk Spidroin
复制标题
DOI：
10.1021/jp991363s
复制
发表时间：
1999-12
影响因子：
3.3
通讯作者：
R. Valluzzi;S. Szela;P. Avtges;and D. Kirschner;D. Kaplan
中科院分区：
文献类型：
--
作者：
R. Valluzzi;S. Szela;P. Avtges;and D. Kirschner;D. Kaplan
The formation of intractable β-sheet crystallites is a major cause of insolubility in proteins that can form β-sheets. To study this phenomenon, recombinant DNA techniques were used to prepare a protein modeling the consensus sequence of Nephila clavipes spider dragline silk, incorporating redox “triggering” residues. X-ray diffraction, electron diffraction, transmission electron microscopy (TEM), and Fourier transform infrared spectroscopy (FTIR) were used to characterize the ability of the recombinant protein to form β-sheet crystals dependent on the redox trigger oxidation state. Changes in the crystallinity were observed when triggered (oxidized/soluble) and untriggered (reduced/insoluble) protein samples were compared. The β-sheet content was undetectable in the triggered state, while clear evidence of β-sheet crystallinity was observed in the untriggered state. TEM and electron diffraction data of thin films of the untriggered protein indicated that spontaneous local orientation of needlelike crysta...
