Functional Characterization and NMR Spectroscopy on Full-Length Vpu from HIV-1 Prepared by Total Chemical Synthesis
Kochendoerfer G, Jones D, Lee S, Oblatt-Montal M, Opella S, Montal M. Functional Characterization and NMR Spectroscopy on Full-Length Vpu from HIV-1 Prepared by Total Chemical Synthesis. Journal Of The American Chemical Society 2004, 126: 2439-2446. PMID: 14982452, DOI: 10.1021/ja038985i.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceHIV-1Human Immunodeficiency Virus ProteinsIon ChannelsLipid BilayersMicellesMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularRecombinant ProteinsViral Regulatory and Accessory ProteinsConceptsTotal chemical synthesisChemical synthesisNMR spectroscopyNative chemical ligation methodologyMembrane proteinsSolid-phase peptide synthesisSolid-state NMR spectraRecombinant proteinsPhase peptide synthesisSolution NMR spectroscopyFull-length VpuIntegral membrane proteinsHydrated lipid bilayerHomogeneous membrane proteinsLigation methodologyChemical ligationPeptide synthesisNMR spectraBacterial expressionFunctional characterizationSynthetic proteinsLipid micellesLipid bilayersCharacterization studiesOverall topology