Cargando…
Use of Paramagnetic (19)F NMR to Monitor Domain Movement in a Glutamate Transporter
In proteins where conformational changes are functionally important, the number of accessible states and their dynamics are often difficult to establish. Here we describe a novel (19)F-NMR spectroscopy approach to probe dynamics of large membrane proteins. We labeled a glutamate transporter homologu...
Autores principales: | Huang, Yun, Wang, Xiaoyu, Lv, Guohua, Razavi, Asghar M., Huysmans, Gerard H. M., Weinstein, Harel, Bracken, Clay, Eliezer, David, Boudker, Olga |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7442671/ https://www.ncbi.nlm.nih.gov/pubmed/32514183 http://dx.doi.org/10.1038/s41589-020-0561-6 |
Ejemplares similares
-
Large domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters
por: Wang, Xiaoyu, et al.
Publicado: (2020) -
The high‐energy transition state of the glutamate transporter homologue GltPh
por: Huysmans, Gerard H M, et al.
Publicado: (2020) -
Environmentally Ultrasensitive
Fluorine Probe to Resolve
Protein Conformational Ensembles by (19)F NMR and Cryo-EM
por: Huang, Yun, et al.
Publicado: (2023) -
Single-molecule transport kinetics of a glutamate transporter homolog shows static disorder
por: Ciftci, Didar, et al.
Publicado: (2020) -
Symport and antiport mechanisms of human glutamate transporters
por: Qiu, Biao, et al.
Publicado: (2023)