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Proteoliposome Proton Flux Assays Establish Net Conductance, Ph-Sensitivity, And Functional Integrity Of A Novel Truncate Of The M2 Ion "Channel" Of Influenza A, Emily Peterson
Theses and Dissertations
A novel truncate of Influenza A M2 protein (residues 22-62), incorporated into a uniquely tailored proteoliposome proton uptake assay, demonstrated proton flux more characteristic of an ion transporter than a traditional ion "channel." The liposome paradigm was essential for testing the conductance activity of this M2 truncate at a range of extraphysiological pHs appropriate for channel vs. transport function determination. In addition to transporter-typical proton flux, M2(22-62) showed the key characteristics of functional integrity: selective proton uptake into liposomes and block of uptake by amantadine. Two sets of proteoliposome proton flux assays were carried out, Set 1 at pH values …
Properties Of Conductance And Inhibition Of Proton Channels: M2 From Influenza A Virus And Fo From Escherichia Coli Atp Synthase, Jeffrey C. Moffat
Properties Of Conductance And Inhibition Of Proton Channels: M2 From Influenza A Virus And Fo From Escherichia Coli Atp Synthase, Jeffrey C. Moffat
Theses and Dissertations
Proton channels are essential for many of the processes of life. The influenza A viral protein M2 is responsible for sensing the conditions necessary for viral RNA release. The proton-translocating FoF1 ATPase (ATP synthase) uses a proton gradient to drive adenosine triphosphate (ATP) synthesis. We have directly measured proton uptake in vesicles containing reconstituted M2 or FO by monitoring external pH after addition of valinomycin to vesicles with 100-fold diluted external [K+]. This proton flux assay was utilized to quantify proton flux through single M2 and Fo channels. Contrary to previous reports, proton uptake by M2 was not significantly altered …