Difference between revisions of "Part:BBa K5396002"
Jocomodaro (Talk | contribs) |
Jocomodaro (Talk | contribs) |
||
| Line 8: | Line 8: | ||
=== Usage and Biology === | === Usage and Biology === | ||
<p>Spidroins are the primary proteins that compose spider silk, renowned for their exceptional mechanical properties, including strength, elasticity, and biodegradability. These proteins are produced in specialized glands of spiders and it can have various functions, such as web construction, prey capture, and mobility.</p> | <p>Spidroins are the primary proteins that compose spider silk, renowned for their exceptional mechanical properties, including strength, elasticity, and biodegradability. These proteins are produced in specialized glands of spiders and it can have various functions, such as web construction, prey capture, and mobility.</p> | ||
| − | <p>Spidroins are characterized by repetitive amino acid sequences that contribute to their unique structural properties. They typically consist of two main domains:</p> | + | <p>[https://pubs.acs.org/doi/10.1021/bm401709v] Spidroins are characterized by repetitive amino acid sequences that contribute to their unique structural properties. They typically consist of two main domains:</p> |
<ul> | <ul> | ||
<li><b>N-terminal domain (Nt):</b> This region is involved in the initial formation of silk fibers and is crucial for the protein's solubility and stability.</li> | <li><b>N-terminal domain (Nt):</b> This region is involved in the initial formation of silk fibers and is crucial for the protein's solubility and stability.</li> | ||
| − | <li><b>C-terminal domain (Ct):</b> This domain plays a significant role in the dimerization of spidroins and helps prevent aggregation during storage. The | + | <li><b>C-terminal domain (Ct):</b> This domain plays a significant role in the dimerization of spidroins and helps prevent aggregation during storage. The Ct has been shown to adopt a dimeric folding structure that is conserved across different types of spidroins, indicating a common functional role in silk formation</li> |
</ul> | </ul> | ||
| + | <p>The repetitive sequences within spidroins often contain motifs rich in glycine and alanine, which facilitate the formation of β-sheet structures that enhance the mechanical properties of the silk fibers. </p> | ||
<p><b>NT2RepCT</b> is a recombinant miniature spidroin protein that has been engineered to mimic the properties of natural spider silk proteins. It is composed of several key domains that enable it to self-assemble into hydrogels and fibers under the right conditions [ ].</p> | <p><b>NT2RepCT</b> is a recombinant miniature spidroin protein that has been engineered to mimic the properties of natural spider silk proteins. It is composed of several key domains that enable it to self-assemble into hydrogels and fibers under the right conditions [ ].</p> | ||
<!-- --> | <!-- --> | ||
Revision as of 11:19, 20 September 2024
Nt2RepCt-SpyTag
This Nt2RepCt protein has a SpyTag, a 13-amino-acid peptide that is part of the SpyCatcher-SpyTag system, which can enable irreversible protein conjugation.
This part was used as template to construct BBa_K5396005, BBa_K5396006, BBa_K5396009 and BBa_K5396010.
Usage and Biology
Spidroins are the primary proteins that compose spider silk, renowned for their exceptional mechanical properties, including strength, elasticity, and biodegradability. These proteins are produced in specialized glands of spiders and it can have various functions, such as web construction, prey capture, and mobility.
[1] Spidroins are characterized by repetitive amino acid sequences that contribute to their unique structural properties. They typically consist of two main domains:
- N-terminal domain (Nt): This region is involved in the initial formation of silk fibers and is crucial for the protein's solubility and stability.
- C-terminal domain (Ct): This domain plays a significant role in the dimerization of spidroins and helps prevent aggregation during storage. The Ct has been shown to adopt a dimeric folding structure that is conserved across different types of spidroins, indicating a common functional role in silk formation
The repetitive sequences within spidroins often contain motifs rich in glycine and alanine, which facilitate the formation of β-sheet structures that enhance the mechanical properties of the silk fibers.
NT2RepCT is a recombinant miniature spidroin protein that has been engineered to mimic the properties of natural spider silk proteins. It is composed of several key domains that enable it to self-assemble into hydrogels and fibers under the right conditions [ ].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 895
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]