Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel-Reference-Cited by-同舟云学术

Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel

Published:2016 Issue:41 Volume:18 Page:28939-28950
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Markiewicz Beatrice N.¹²³⁴,Lemmin Thomas⁵⁶⁷⁴,Zhang Wenkai⁸²³⁴,Ahmed Ismail A.⁹²³⁴,Jo Hyunil⁵⁶⁷⁴,Fiorin Giacomo¹⁰¹¹³⁴,Troxler Thomas¹²³⁴⁸,DeGrado William F.⁵⁶⁷⁴,Gai Feng¹²³⁴⁸

Affiliation:

1. Department of Chemistry

2. University of Pennsylvania

3. Philadelphia

4. USA

5. Department of Pharmaceutical Chemistry

6. University of California San Francisco

7. San Francisco

8. Ultrafast Optical Processes Laboratory

9. Department of Biochemistry and Biophysics

10. Institute for Computational Molecular Science

11. Temple University

Abstract

The Trp41 tetrad of the M2 proton channel is found to be relatively dehydrated even at pH 5, indicative of the existence of an additional barrier for proton conduction.

Funder

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CP/C6CP03426H

Reference75 articles.

1. Ion selectivity and activation of the M2 ion channel of influenza virus

2. The M2 Proton Channels of Influenza A and B Viruses

3. Structure and mechanism of the M2 proton channel of influenza A virus