Difference between revisions of "Part:BBa K4438800"
Neha adarsh (Talk | contribs) |
|||
| (One intermediate revision by one other user not shown) | |||
| Line 5: | Line 5: | ||
Aptamer_MN4 is a single-stranded DNA aptamer having 36 nucleotides. Figure 1A) shows the secondary structure and minimum free energy. | Aptamer_MN4 is a single-stranded DNA aptamer having 36 nucleotides. Figure 1A) shows the secondary structure and minimum free energy. | ||
| − | + | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
| + | This part binds to cocaine with KD being 7 ± 1 uM (calculated using Isothermal Titration Calorimetry). It has three stems that are arranged around a three-way junction. Mostly used as a proof-of-concept aptamer. It also binds to other alkaloids. Its affinity for quinine is 30 times more than that of cocaine, with KD being 0.23 ± 0.03 uM. Since the same aptamer binds to many ligands, this part is unsuitable for biosensing applications [1,2]. | ||
| + | [[File:T--IISER-Tirupati_India--mn4structure7.png]] | ||
<!-- --> | <!-- --> | ||
| Line 17: | Line 19: | ||
<partinfo>BBa_K4438800 parameters</partinfo> | <partinfo>BBa_K4438800 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
| + | ===References=== | ||
| + | [1].Reinstein, O., Yoo, M., Han, C., Palmo, T., Beckham, S. A., Wilce, M. C., & Johnson, P. E. (2013). Quinine binding by the cocaine-binding aptamer. Thermodynamic and hydrodynamic analysis of high-affinity binding of an off-target ligand. Biochemistry, 52(48), 8652-8662. | ||
| + | [2].Neves, M. A., Reinstein, O., & Johnson, P. E. (2010). Defining a stem length-dependent binding mechanism for the cocaine-binding aptamer. A combined NMR and calorimetry study. Biochemistry, 49(39), 8478-8487. | ||
Latest revision as of 18:24, 13 October 2022
Aptamer_MN4
Aptamer_MN4 is a single-stranded DNA aptamer having 36 nucleotides. Figure 1A) shows the secondary structure and minimum free energy.
Usage and Biology
This part binds to cocaine with KD being 7 ± 1 uM (calculated using Isothermal Titration Calorimetry). It has three stems that are arranged around a three-way junction. Mostly used as a proof-of-concept aptamer. It also binds to other alkaloids. Its affinity for quinine is 30 times more than that of cocaine, with KD being 0.23 ± 0.03 uM. Since the same aptamer binds to many ligands, this part is unsuitable for biosensing applications [1,2].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
[1].Reinstein, O., Yoo, M., Han, C., Palmo, T., Beckham, S. A., Wilce, M. C., & Johnson, P. E. (2013). Quinine binding by the cocaine-binding aptamer. Thermodynamic and hydrodynamic analysis of high-affinity binding of an off-target ligand. Biochemistry, 52(48), 8652-8662. [2].Neves, M. A., Reinstein, O., & Johnson, P. E. (2010). Defining a stem length-dependent binding mechanism for the cocaine-binding aptamer. A combined NMR and calorimetry study. Biochemistry, 49(39), 8478-8487.