Team:Groningen/Silk/Protein

From 2013.igem.org

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<h1>Silk protein</h1>
<h1>Silk protein</h1>
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The spider silk protein is a fibrous protein. It does not have a folded state on its own; it is able to assemble (multimerize) with multiple identical proteins to form the silk. The protein consists of roughly 3 motifs, each featuring a particular secondary structure in the assembly (table 1) (ref 11 paper recomb biomaterials).  
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The spider silk protein is a fibrous protein. It does not have a folded state on its own; it is able to assemble (multimerize) with multiple identical proteins to form the silk. The protein consists of roughly 3 motifs, each featuring a particular secondary structure in the assembly (table 1) (<b>ref 11</b> paper recomb biomaterials).  
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<td>Amino acid sequence</td>
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<th>Amino acid sequence</th>
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<td>Secondary structure</td>
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<th>Secondary structure</th>
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<td>Properties</td>
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<th>Properties</th>
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<font size="1">Table 1, Spider silk protein motifs</font><br><br>
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In order to make the silk material a large amount of these proteins are required. The protein has a very repetitive nature (fig. X), with these motifs (table 1) recurring within the protein. This is difficult to produce, because it requires presence of the same tRNAs in a large amount. This can be solved with codon optimization. See ‘Codon optimization’ (link) at the modelling section for the explanation of this approach.
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In order to make the silk material a large amount of these proteins are required. The protein has a very repetitive nature (fig. 2), with these motifs (table 1) recurring within the protein. This is difficult to produce, because it requires presence of the same tRNAs in a large amount. This can be solved with codon optimization. See ‘Codon optimization’ (link) at the modelling section for the explanation of this approach.
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<font size="1">Figure 2, Major ampullate Spidroin 2 (MaSp2) from <i>Argiope aurantia</i></font>
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Revision as of 13:48, 4 October 2013

Silk protein

The spider silk protein is a fibrous protein. It does not have a folded state on its own; it is able to assemble (multimerize) with multiple identical proteins to form the silk. The protein consists of roughly 3 motifs, each featuring a particular secondary structure in the assembly (table 1) (ref 11 paper recomb biomaterials).

Depending on the processing of the silk proteins, it can have a degree of these secondary structures, defining its properties (table 1). This characteristic of the silk proteins will be discussed in detail in the ‘Silk protein’(link) section.


Amino acid sequence Secondary structure Properties
AAAAAAAA β-sheet Tensile strenght, rigidity, hydrophobicity
GPG(AG)QQ / GPG(SGG)QQ / GPGGX β-spiral / β-turn Extensibility, elasticity
GGX 310 helix Link, alignment, flexibility
Table 1, Spider silk protein motifs

In order to make the silk material a large amount of these proteins are required. The protein has a very repetitive nature (fig. 2), with these motifs (table 1) recurring within the protein. This is difficult to produce, because it requires presence of the same tRNAs in a large amount. This can be solved with codon optimization. See ‘Codon optimization’ (link) at the modelling section for the explanation of this approach.


Figure 2, Major ampullate Spidroin 2 (MaSp2) from Argiope aurantia

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