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

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

80 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
Externally published	Yes

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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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.",

keywords = "M2 protein, NMR spectroscopy, membrane proteins, structural biology, structural validation",

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

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language = "English (US)",

volume = "51",

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journal = "Angewandte Chemie - International Edition",

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T1 - M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes

AU - Miao, Yimin

AU - Qin, Huajun

AU - Fu, Riqiang

AU - Sharma, Mukesh

AU - Can, Thach V.

AU - Hung, Ivan

AU - Luca, Sorin

AU - Gor'Kov, Peter L.

AU - Brey, William W.

AU - Cross, Timothy A.

PY - 2012/8/13

Y1 - 2012/8/13

N2 - 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.

AB - 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.

KW - M2 protein

KW - NMR spectroscopy

KW - membrane proteins

KW - structural biology

KW - structural validation

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JO - Angewandte Chemie - International Edition

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SN - 1433-7851

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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