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
1999
Solution structure of neuromedin B by 1H nuclear magnetic resonance spectroscopy
Lee S, Kim Y. Solution structure of neuromedin B by 1H nuclear magnetic resonance spectroscopy. FEBS Letters 1999, 460: 263-269. PMID: 10544247, DOI: 10.1016/s0014-5793(99)01346-0.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonance spectroscopySDS micellesMagnetic resonance spectroscopyTwo-dimensional nuclear magnetic resonance spectroscopyResonance spectroscopyAromatic ring protonsSolution structureMembrane-mimicking environmentHydrophobic acyl chainsStructure-activity relationshipsMethylene protonsLongitudinal relaxation dataNOESY experimentsHelical conformationConformational featuresRing protonsMicellesMolecular mechanismsSpectroscopyAcyl chainsExtrinsic interactionsRelaxation dataEfficient drugsResiduesProtons