| Autor: |
Janire Urrutia, Aguado, Alejandra, Gomis-Perez, Carolina, Muguruza-Montero, Arantza, Ballesteros, Oscar R., Jiaren Zhang, Nuñez, Eider, Covadonga Malo, Chung, Hee Jung, Aritz Leonardo, Bergara, Aitor, Villarroel, Alvaro |
| Rok vydání: |
2021 |
| DOI: |
10.6084/m9.figshare.14643274.v1 |
| Popis: |
Additional file 1: Figure S1. Relationship between normalized current densities from cells expressing Kv7.2 channels carrying the indicated mutations in the helix A. Figure S2. The W344R mutation reduced expression of CFP-Kv7.2 in cultured hippocampal neurons. Figure S3. I340E and W344R mutants severely reduced surface and total expression of heteromeric HA-Kv7.3/CFP-Kv7.2 in the axons of cultured hippocampal neurons. Figure S4. Background-subtracted fluorescent intensities of surface HA-Kv7.3 in different compartments of cultured hippocampal neurons. Figure S5. Cartoon representation of a Kv7 channel. Figure S6. Emission spectra of the purified mTFP1-AB-mcpVenus/CaM complex in the presence of increasing concentrations of the denaturant urea. Figure S7. Emission spectra of the soluble WT and W344R mTFP1-AB-mcpVenus proteins translated in CaM-free non-denaturing conditions. Figure S8. Fluorescent image of a SDS-PAGE of unboiled bacterial extracts of cells expressing WT or W344R mTFP1-AB-mcpVenus proteins, expressed at 18°C. Figure S9. Schematic representation of the constructs used for in vivo translation and representative fluorescent images of SDS-PAGE gels loaded with unboiled bacterial extracts expressing WT-AP construct with and without CaM. Figure S10. Relationship between current densities of homomeric Kv7.2 channels carrying the indicated mutations at position 344 and the computed binding energies in Rosetta Energy Units. Figure S11. Time series of the angle of Tryptophan 344 through a molecular dynamics simulation of the Kv7.2 WT CRD forced to start in T configuration. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
