2003
Structures of neuropeptide γ from goldfish and mammalian neuropeptide γ, as determined by 1H NMR spectroscopy
Lee K, Lee S, Kim Y, Park NG. Structures of neuropeptide γ from goldfish and mammalian neuropeptide γ, as determined by 1H NMR spectroscopy. Chemical Biology & Drug Design 2003, 61: 274-285. PMID: 12662361, DOI: 10.1034/j.1399-3011.2003.00058.x.Peer-Reviewed Original ResearchConceptsAmino acid sequenceN-terminal regionAlpha-helical conformationAqueous TFE solutionAcid sequenceShort helixAlpha-helical structureC-terminal regionTerminal amino acid sequencePost-translational processingBeta-turn regionMammalian systemsTFE solutionC-terminusMet21Solution structureNeuropeptide γHelixBiological responsesGold fishBiological actionsSodium dodecyl sulfate micellesHis12Nuclear magnetic resonance spectroscopyNeuropeptide gamma
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
Comparison of the Structures of β Amyloid Peptide (25–35) and Substance P in Trifluoroethanol/Water Solution
Lee S, Suh Y, Kim S, Kim Y. Comparison of the Structures of β Amyloid Peptide (25–35) and Substance P in Trifluoroethanol/Water Solution. Journal Of Biomolecular Structure And Dynamics 1999, 17: 381-391. PMID: 10563586, DOI: 10.1080/07391102.1999.10508369.Peer-Reviewed Original ResearchConceptsSubstance PTrifluoroethanol/water solutionTachykinin familyAmyloid peptidesBrains of patientsHydrophobic side chainsBeta-amyloid peptideNMR spectroscopyAqueous solutionΒ-amyloid peptideAlpha-helical structureAromatic ringConformational featuresWater solutionSide chainsTachykinin receptorsBeta amyloidSenile plaquesAlzheimer's diseaseThree-dimensional structureDiseaseReceptors