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. 2015 Mar;6(3):229-33.
doi: 10.1007/s13238-014-0129-x.

Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using (19)F nuclear magnetic resonance

Dong Li  1 , Juan Li, Yonglong Zhuang, Longhua Zhang, Ying Xiong, Pan Shi, Changlin Tian
Affiliations

Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using (19)F nuclear magnetic resonance

Dong Li et al. Protein Cell. 2015 Mar.
No abstract available

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Figures

Figure 1
Figure 1
F2Y was incorporated at Tyr574 site of ETK-FL protein. (A) Topology diagram of an ETK protein in lipid bilayer, containing two transmembrane helices and a cytosolic tyrosine kinase domain including the auto-phosphorylation site Y574 and tyrosine rich C-terminal tail; (B) Coomassie blue staining of purified ETK-Y574F2Y; (C) Western-blot of purified ETK-Y574F2Y
Figure 2
Figure 2
SMA wrapped uni-lamellar liposome elevated phosphorylation level of ETK-FL-Y574-F2Y. (A) Topology diagram of an ETK-FL in multi-lamellar lipid bilayer vesicles, composition of poly-SMA and topology diagram of an ETK protein in lipodisq; (B) Transmission electron microscopy pictures of native E. coli liposomes after freeze-thaw-bath sonication with addition of 0, 10, 30 μL poly-SMA3000 (3:1). The 0.2 μm bar was shown in the same size in the three pictures. (C) 19F NMR spectrum of ETK-Y574F2Y in native liposome with the presence of PTP1B; (D) 19F NMR spectrum of ETK-Y574F2Y in native liposome with the presence of ATP and Mg2+; (E) 19F NMR spectrum of ETK-Y574-F2Y in lipodisq with the presence of PTP1B; (F) 19F NMR spectrum of ETK-Y574F2Y in lipodisq with the presence of ATP and Mg2+
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