In situ 19F NMR studies of an E. coli membrane protein.

Protein Science : a Publication of the Protein Society
Pan ShiChanglin Tian

Abstract

In this report, (19)F spin incorporation in a specific site of a specific membrane protein in E. coli was accomplished via trifluoromethyl-phenylalanine ((19) F-tfmF). Site-specific (19)F chemical shifts and longitudinal relaxation times of diacylglycerol kinase (DAGK), an E. coli membrane protein, were measured in its native membrane using in situ magic angle spinning (MAS) solid state nuclear magnetic resonance (NMR). Comparing with solution NMR data of the purified DAGK in detergent micelles, the in situ MAS-NMR data illustrated that (19)F chemical shift values of residues at different membrane protein locations were influenced by interactions between membrane proteins and their surrounding lipid or lipid mimic environments, while (19)F side chain longitudinal relaxation values were probably affected by different interactions of DAGK with planar lipid bilayer versus globular detergent micelles.

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Citations

Mar 14, 2012·Proceedings of the National Academy of Sciences of the United States of America·Gary J Pielak, Fang Tian
Jun 5, 2014·Annual Review of Biophysics·Darón I Freedberg, Philipp Selenko
Feb 9, 2018·Chemistry : a European Journal·Roman M BychekPavel K Mykhailiuk
Apr 21, 2019·Biological Chemistry·Dania Rose-SperlingUte A Hellmich
Jun 13, 2019·Current Medicinal Chemistry·Cong Bao Kang
Jul 19, 2013·Chemical Society Reviews·Han ChenLing Peng
Mar 17, 2017·Annual Review of Analytical Chemistry·Conggang LiMaili Liu
Dec 8, 2020·Biophysical Journal·Fatemeh Azadi-ChegeniAnjali Pandit
Oct 2, 2021·Journal of the American Chemical Society·Xiaoyan WangJiangyun Wang

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