M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes

Yimin Miao; Huajun Qin; Riqiang Fu; Mukesh Sharma; Thach V. Can; Ivan Hung; Sorin Luca; Peter L. Gor'Kov; William W. Brey; Timothy A. Cross

doi:10.1002/anie.201204666

M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes

Yimin Miao, Huajun Qin, Riqiang Fu, Mukesh Sharma, Thach V. Can, Ivan Hung, Sorin Luca, Peter L. Gor'Kov, William W. Brey, Timothy A. Cross

Pharmaceutical Science

Research output: Contribution to journal › Article › peer-review

74 Scopus citations

Abstract

Validation: Membrane protein structures are sensitive to the environment used for structural characterization. NMR spectra of the full-length M2 proton channel from influenza A were measured directly in E. coli membranes and compared to spectra of the protein in synthetic lipid bilayers. The results demonstrate that these bilayers provide a native-like membrane environment.

Original language	English (US)
Pages (from-to)	8383-8386
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	33
DOIs	https://doi.org/10.1002/anie.201204666
State	Published - Aug 13 2012

Keywords

M2 protein
NMR spectroscopy
membrane proteins
structural biology
structural validation

ASJC Scopus subject areas

Catalysis
Chemistry(all)

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10.1002/anie.201204666

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M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes. / Miao, Yimin; Qin, Huajun; Fu, Riqiang; Sharma, Mukesh; Can, Thach V.; Hung, Ivan; Luca, Sorin; Gor'Kov, Peter L.; Brey, William W.; Cross, Timothy A.

In: Angewandte Chemie - International Edition, Vol. 51, No. 33, 13.08.2012, p. 8383-8386.

Research output: Contribution to journal › Article › peer-review

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AU - Hung, Ivan

AU - Luca, Sorin

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