M2 Proton Channel Structural Validation from Full‐Length Protein Samples in Synthetic Bilayers and  E. coli  Membranes | Zendy

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

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

M2 Proton Channel Structural Validation from Full‐Length Protein Samples in Synthetic Bilayers and E. coli Membranes

Author(s) -

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.

Publication year - 2012

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201204666

Subject(s) - membrane , lipid bilayer , characterization (materials science) , chemistry , membrane protein , bilayer , biophysics , analytical chemistry (journal) , materials science , biochemistry , chromatography , nanotechnology , biology

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research