Solid-State 19F NMR Spectroscopy Reveals That Trp41 Participates in the Gating Mechanism of the M2 Proton Channel of Influenza A Virus-Reference-Cited by-同舟云学术

Solid-State 19F NMR Spectroscopy Reveals That Trp41 Participates in the Gating Mechanism of the M2 Proton Channel of Influenza A Virus

Published:2007-12-29 Issue:3 Volume:130 Page:918-924
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Witter Raiker¹,Nozirov Farhod¹,Sternberg Ulrich¹,Cross Timothy A.¹,Ulrich Anne S.¹,Fu Riqiang¹

Affiliation:

1. Forschungszentrum Karlsruhe, IBG, POB 3640, 76021 Karlsruhe, Germany, National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, Florida 32310, Department of Chemistry and Biochemistry, Institute of Biophysics, Florida State University, Tallahassee, Florida 32306, and Institut für Organische Chemie, University of Karlsruhe, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0754305

Reference51 articles.

1. The Grotthuss mechanism

2. Influenza virus M2 protein has ion channel activity

3. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer

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