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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Detalles Bibliográficos
Autores principales: Liu, Qi, He, Qing-tao, Lyu, Xiaoxuan, Yang, Fan, Zhu, Zhong-liang, Xiao, Peng, Yang, Zhao, Zhang, Feng, Yang, Zhao-ya, Wang, Xiao-yan, Sun, Peng, Wang, Qian-wen, Qu, Chang-xiu, Gong, Zheng, Lin, Jing-yu, Xu, Zhen, Song, Shao-le, Huang, Shen-ming, Guo, Sheng-chao, Han, Ming-jie, Zhu, Kong-kai, Chen, Xin, Kahsai, Alem W., Xiao, Kun-Hong, Kong, Wei, Li, Fa-hui, Ruan, Ke, Li, Zi-jian, Yu, Xiao, Niu, Xiao-gang, Jin, Chang-wen, Wang, Jiangyun, Sun, Jin-peng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7519161/
https://www.ncbi.nlm.nih.gov/pubmed/32978402
http://dx.doi.org/10.1038/s41467-020-18433-5

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7519161/
https://www.ncbi.nlm.nih.gov/pubmed/32978402
http://dx.doi.org/10.1038/s41467-020-18433-5

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