Photoinduced Electron Transfer and Fluorophore Motion as a Probe of the Conformational Dynamics of Membrane Proteins: Application to the Influenza A M2 Proton Channel

• Published in: Langmuir Vol. 27; no. 7; pp. 3815 - 3821
• Main Authors: Rogers, Julie M. G, Polishchuk, Alexei L, Guo, Lin, Wang, Jun, DeGrado, William F, Gai, Feng
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 05.04.2011
• Subjects: Biological Interfaces: Biocolloids, Biomolecular and Biomimetic Materials; Chemistry; Colloidal state and disperse state; Exact sciences and technology; Fluorescence; General and physical chemistry; Hydrogen-Ion Concentration; Liposomes - chemistry; Membrane Proteins - chemistry; Porous materials; Protein Conformation; Spectrometry, Fluorescence - methods; Unilamellar Liposomes - chemistry; Viral Matrix Proteins - chemistry; Binding; Drug; Structure function; Motion; Fluctuations; Dyes; Conformational dynamics; Fluorescence; Electron transfer; Tryptophan; Equilibrium; Porous material; Mechanism; Protein; Fluorophore; Pore; Residue; Proton; pH; Models; Inhibition; Conformational transition

The structure and function of the influenza A M2 proton channel have been the subject of intensive investigations in recent years because of their critical role in the life cycle of the influenza virus. Using a truncated version of the M2 proton channel (i.e., M2TM) as a model, here we show that flu...