2004
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 ResearchConceptsTotal 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
2000
Role of the Hinge Region and the Tryptophan Residue in the Synthetic Antimicrobial Peptides, Cecropin A(1−8)−Magainin 2(1−12) and Its Analogues, on Their Antibiotic Activities and Structures † , ‡
Oh D, Shin S, Lee S, Kang J, Kim S, Ryu P, Hahm K, Kim Y. Role of the Hinge Region and the Tryptophan Residue in the Synthetic Antimicrobial Peptides, Cecropin A(1−8)−Magainin 2(1−12) and Its Analogues, on Their Antibiotic Activities and Structures † , ‡. Biochemistry 2000, 39: 11855-11864. PMID: 11009597, DOI: 10.1021/bi000453g.Peer-Reviewed Original ResearchAmino Acid SequenceAmino Acid SubstitutionAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntineoplastic AgentsBacillus subtilisElectric ConductivityEscherichia coliHumansIon ChannelsJurkat CellsK562 CellsLipid BilayersMagaininsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryProtein Structure, TertiaryTryptophanXenopus Proteins