Article
Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog.
Nature chemical biology - 1 Sept 2020
Huang Yun, Wang Xiaoyu, Lv Guohua, Razavi Asghar M, Huysmans Gerard H M, Weinstein Harel, Bracken Clay, Eliezer David, Boudker Olga
Abstract excerpt
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 19F-NMR spectroscopy approach to probe dynamics of large membrane proteins. We labeled a glutamate transporter homolog with a 19F probe via cysteine chemistry and with a Ni2+ ion via chelation by a di-histidine motif. We used...
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