Difference between revisions of "Part:BBa K2719000:Design"
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===Source=== | ===Source=== | ||
| − | + | This part was synthesized by IDT. | |
===References=== | ===References=== | ||
| − | Chakrabartty, Baldwin. (1995). Stability of alpha-Helix. October 16, 2018, of Science Direct Website: https://www.sciencedirect.com/science/article/pii/S0065323308603344 | + | <p>Chakrabartty, Baldwin. (1995). <i>Stability of alpha-Helix</i>. October 16, 2018, of Science Direct Website: https://www.sciencedirect.com/science/article/pii/S0065323308603344</p> |
| + | <p>Harper S. & Speicher D. (2010). Purification of proteins fused to glutathione S-transferase. <i> Protein Chromatography </i>. Doi: 10.1007/978-1-60761-913-0_14.</p> | ||
Latest revision as of 02:23, 18 October 2018
GST
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 85
Design Notes
GST coding sequence is the one that is use for give structure and stability to Tenascin domain V. The binding is created by a polyproline linker which is going to maintain the original three dimensional structure of the tenascin domain V. GST has a high level of stability because of its structure and we can see it in figure 1. Its structure is mainly composed by alpha-helix structures giving it more stability to it structure. (Chakrabartty and Baldwin, 1995)
"
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Figure 1. GST 3D structure , modelled with Swiss-Model
Source
This part was synthesized by IDT.
References
Chakrabartty, Baldwin. (1995). Stability of alpha-Helix. October 16, 2018, of Science Direct Website: https://www.sciencedirect.com/science/article/pii/S0065323308603344
Harper S. & Speicher D. (2010). Purification of proteins fused to glutathione S-transferase. Protein Chromatography . Doi: 10.1007/978-1-60761-913-0_14.