Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1768, Issue 12, Pages 3162-3170Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2007.08.025
Keywords
M2 channel; influenza A virus; conformational plasticity; PISEMA; solid-state NMR; membrane protein
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Funding
- NIAID NIH HHS [R01 AI023007-23, R01 AI073891, AI 23007, R01 AI023007] Funding Source: Medline
- NIGMS NIH HHS [P01 GM064676-03, P01 GM064676-01, P01 GM064676-02, P01 GM064676, P01 GM064676-04, P01 GM064676-05] Funding Source: Medline
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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. (C) 2007 Elsevier B.V. All rights reserved.
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