Cloning and Expression of Spider Dragline Silk Protein Gene in Escherichia coli and Eukaryotic Cells

2011 ◽  
Author(s):  
Li Wenli
Keyword(s):  
Escherichia Coli ◽  
Protein Gene ◽  
Silk Protein ◽  
Cloning And Expression ◽  
Eukaryotic Cells ◽  
Dragline Silk ◽  
Spider Dragline Silk

scholarly journals Nanostructure and molecular mechanics of spider dragline silk protein assemblies

2010 ◽  
Vol 7 (53) ◽  
pp. 1709-1721 ◽  
Author(s):  
Sinan Keten ◽  
Markus J. Buehler
Keyword(s):  
Secondary Structure ◽  
Spider Silk ◽  
Mechanical Performance ◽  
Experimental Studies ◽  
Silk Protein ◽  
Nephila Clavipes ◽  
Protein Assemblies ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Secondary Structure Content

Spider silk is a self-assembling biopolymer that outperforms most known materials in terms of its mechanical performance, despite its underlying weak chemical bonding based on H-bonds. While experimental studies have shown that the molecular structure of silk proteins has a direct influence on the stiffness, toughness and failure strength of silk, no molecular-level analysis of the nanostructure and associated mechanical properties of silk assemblies have been reported. Here, we report atomic-level structures of MaSp1 and MaSp2 proteins from the Nephila clavipes spider dragline silk sequence, obtained using replica exchange molecular dynamics, and subject these structures to mechanical loading for a detailed nanomechanical analysis. The structural analysis reveals that poly-alanine regions in silk predominantly form distinct and orderly beta-sheet crystal domains, while disorderly regions are formed by glycine-rich repeats that consist of 3 1 -helix type structures and beta-turns. Our structural predictions are validated against experimental data based on dihedral angle pair calculations presented in Ramachandran plots, alpha-carbon atomic distances, as well as secondary structure content. Mechanical shearing simulations on selected structures illustrate that the nanoscale behaviour of silk protein assemblies is controlled by the distinctly different secondary structure content and hydrogen bonding in the crystalline and semi-amorphous regions. Both structural and mechanical characterization results show excellent agreement with available experimental evidence. Our findings set the stage for extensive atomistic investigations of silk, which may contribute towards an improved understanding of the source of the strength and toughness of this biological superfibre.

scholarly journals Cloning and Expression of an Insecticidal k-73 Type Crystal Protein Gene from Bacillus thuringiensis var. kurstaki into Escherichia coli

1985 ◽  
Vol 50 (3) ◽  
pp. 623-628 ◽  
Author(s):  
James H. McLinden ◽  
Josanne R. Sabourin ◽  
Burton D. Clark ◽  
Diana R. Gensler ◽  
Wesley E. Workman ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacillus Thuringiensis ◽  
Protein Gene ◽  
Crystal Protein ◽  
Cloning And Expression ◽  
Type Crystal

Construct Synthetic Gene Encoding Artificial Spider Dragline Silk Protein and its Expression in Milk of Transgenic Mice

2007 ◽  
Vol 18 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Hong-Tao Xu ◽  
Bao-Liang Fan ◽  
Shu-Yang Yu ◽  
Yin-Hua Huang ◽  
Zhi-Hui Zhao ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Silk Protein ◽  
Synthetic Gene ◽  
Gene Encoding ◽  
Dragline Silk ◽  
Spider Dragline Silk

scholarly journals Super Bacteria: A New Hope of Manufacturing Spider Silk in an Efficient Way

2021 ◽  
Vol 8 (2) ◽  
pp. 225-226
Author(s):  
Chandrayee Talukdar ◽  
Swastik Sastri
Keyword(s):  
Escherichia Coli ◽  
Spider Silk ◽  
Huge Amount ◽  
Dragline Silk ◽  
Synthetic Genes ◽  
Spider Dragline Silk ◽  
Split Intein ◽  
Microbial System ◽  
Simple Product ◽  
Made In

The important properties of spider dragline silk and other protein polymers will find many applications. We have demonstrated the production of spider silk, which has many important properties, are produced from the bacteria including Escherichia coli. The productions of high molecular weight spider drag line encoded by synthetic genes. Silk protein can be efficiently produced by the microbial system has become an advantageous method like quick secretion and simple product recovery has become an efficient method .From the observation of various experiments done by several scientists has shown silk made in laboratory. The study of RIKEN centre for sustainable resource science has shown that spider silk can be produce huge amount. Observation shown that joining of the fragments by split intein sequence  which then cut itself to yield full name protein .Spun into fibers make the microbial spider silk tough , stretchable and stronger. Better modification of bioengineering can increase the amount of production.

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