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DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl (1)H-NMR probe
Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here we report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code expansio...
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| Gepubliceerd in: | Nat Commun |
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| Hoofdauteurs: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Nature Publishing Group UK
2020
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7519161/ https://ncbi.nlm.nih.gov/pubmed/32978402 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-020-18433-5 |
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