Team:Groningen/Silk/Protein

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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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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.
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Depending on the processing of the silk proteins, it can have a degree of these secondary structures, defining its properties (table 1).
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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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<img src="https://static.igem.org/mediawiki/2013/9/95/Masp2.jpg" width="100%">
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<font size="1">Figure 2, Major ampullate Spidroin 2 (MaSp2) from <i>Argiope aurantia</i></font>
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Latest revision as of 17:23, 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).


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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