tetano
Editor, Senior Moderator
Chem Commun (Camb). 2018 May 23. doi: 10.1039/c8cc01533c. [Epub ahead of print]
[h=1]Influenza A M2 transmembrane domain tunes its conformational heterogeneity and structural plasticity in the lipid bilayer by forming loop structures.[/h] Liu Y[SUP]1[/SUP], Tan J[SUP]1[/SUP], Zhang J[SUP]1[/SUP], Li C[SUP]1[/SUP], Luo Y[SUP]1[/SUP], Ye S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] We discovered for the first time that the influenza A virus M2TM tunes its conformational heterogeneity and structural plasticity to respond to environmental cues by undergoing a helix-to-loop transition, resolving controversies regarding the mechanism of proton conduction and plasticity of the M2TM in lipid bilayers.
PMID: 29789823 DOI: 10.1039/c8cc01533c
[h=1]Influenza A M2 transmembrane domain tunes its conformational heterogeneity and structural plasticity in the lipid bilayer by forming loop structures.[/h] Liu Y[SUP]1[/SUP], Tan J[SUP]1[/SUP], Zhang J[SUP]1[/SUP], Li C[SUP]1[/SUP], Luo Y[SUP]1[/SUP], Ye S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] We discovered for the first time that the influenza A virus M2TM tunes its conformational heterogeneity and structural plasticity to respond to environmental cues by undergoing a helix-to-loop transition, resolving controversies regarding the mechanism of proton conduction and plasticity of the M2TM in lipid bilayers.
PMID: 29789823 DOI: 10.1039/c8cc01533c