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      Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel

      , , ,
      Biochimica et Biophysica Acta (BBA) - Biomembranes
      Elsevier BV

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          Abstract

          Membrane protein function within the membrane interstices is achieved by mechanisms that are not typically available to water-soluble proteins. The whole balance of molecular interactions that stabilize three-dimensional structure in the membrane environment is different from that in an aqueous environment. As a result interhelical interactions are often dominated by non-specific van der Waals interactions permitting dynamics and conformational heterogeneity in these interfaces. Here, solid-state NMR data of the transmembrane domain of the M2 protein from influenza A virus are used to exemplify such conformational plasticity in a tetrameric helical bundle. Such data lead to very high resolution structural restraints that can identify both subtle and substantial structural differences associated with various states of the protein. Spectra from samples using two different preparation protocols, samples prepared in the presence and absence of amantadine, and spectra as a function of pH are used to illustrate conformational plasticity.

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          Author and article information

          Journal
          Biochimica et Biophysica Acta (BBA) - Biomembranes
          Biochimica et Biophysica Acta (BBA) - Biomembranes
          Elsevier BV
          00052736
          December 2007
          December 2007
          : 1768
          : 12
          : 3162-3170
          Article
          10.1016/j.bbamem.2007.08.025
          2258276
          17936720
          fb81401c-cc89-415c-81a6-945271b575ed
          © 2007

          https://www.elsevier.com/tdm/userlicense/1.0/

          https://www.elsevier.com/open-access/userlicense/1.0/

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