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• W2015820026 abstract "The solution conformation of alamethicin, a 20-residue antibiotic peptide, has been investigated using two-dimensional n.m.r. spectroscopy. Complete proton resonance assignments of this peptide have been carried out using COSY, SUPERCOSY, RELAY COSY and NOESY two-dimensional spectroscopies. Observation of a large number of nuclear Overhauser effects between sequential backbone amide protons, between backbone amide protons and CβH protons of preceding residues and extensive intramolecular hydrogen bonding patterns of NH protons has established that this polypeptide is in a largely helical conformation. This result is in conformity with earlier reported solid state X-ray results and a recent n.m.r. study in methanol solution (Esposito et al. (1987) Biochemistry26, 1043-1050) but is at variance with an earlier study which favored an extended conformation for the C-terminal half of alamethicin (Bannerjee et al. (1983) J. Mol. Biol.165, 757-775)." @default.
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• W2015820026 date "2009-01-12" @default.
• W2015820026 modified "2023-10-15" @default.
• W2015820026 title "Molecular conformation of alamethicin in dimethylsulfoxide solution" @default.
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• W2015820026 doi "https://doi.org/10.1111/j.1399-3011.1988.tb00931.x" @default.
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