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| - Functional Characterization and NMR Spectroscopy onFull-Length Vpu from HIV-1 Prepared by Total ChemicalSynthesis
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| - Vpu is an 81-residue integral membrane protein encoded in the HIV-1 genome that is ofconsiderable interest because it plays important roles in the release of virus particles from infected cellsand in the degradation of the cellular receptor. We report here the total chemical synthesis of full-lengthVpu(1−81) as well as a site-specifically 15N-labeled analogue, Vpu(2−81), using native chemical ligationmethodologies and also report a structural and functional comparison of these constructs with recombinantprotein obtained via bacterial expression. The structures of the synthetic and expressed polypeptides weresimilar in lipid micelles using solution NMR spectroscopy. Solid-state NMR spectra of the polypeptides inaligned hydrated lipid bilayers indicated that their overall topologies were also very comparable. Further,the channel activity of the synthetic protein was found to be analogous to that previously characterized forthe recombinant protein. We have thus demonstrated that using solid phase peptide synthesis and chemicalligation it is feasible to obtain large quantities of a purified and homogeneous membrane protein in astructurally and functionally relevant form for future structural and characterization studies.
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