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

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72 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 languageEnglish (US)
Pages (from-to)8383-8386
Number of pages4
JournalAngewandte Chemie - International Edition
Volume51
Issue number33
DOIs
StatePublished - Aug 13 2012

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Keywords

  • M2 protein
  • NMR spectroscopy
  • membrane proteins
  • structural biology
  • structural validation

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Cite this

Miao, Y., Qin, H., Fu, R., Sharma, M., Can, T. V., Hung, I., Luca, S., Gor'Kov, P. L., Brey, W. W., & Cross, T. A. (2012). M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes. Angewandte Chemie - International Edition, 51(33), 8383-8386. https://doi.org/10.1002/anie.201204666