Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy

The conformational properties of the magainin family of antimicrobial peptides in aqueous solution and in model membranes have been probed by Fourier transform infrared spectroscopy. The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and...

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Veröffentlicht in:	Biochemistry (Easton) 1992-08, Vol.31 (32), p.7289-7293
Hauptverfasser:	Jackson, Michael, Mantsch, Henry H, Spencer, John H
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Antimicrobial Cationic Peptides Biochemistry & Molecular Biology Biological and medical sciences Dimyristoylphosphatidylcholine Fourier Analysis Fundamental and applied biological sciences. Psychology I.R. spectroscopy Life Sciences & Biomedicine Liposomes magainin 2 Magainins Molecular Sequence Data Oligopeptides - chemistry Peptide Fragments - chemistry Peptides - chemical synthesis Peptides - chemistry Phosphatidylglycerols Protein Conformation Proteins Science & Technology Sequence Homology, Nucleic Acid skin solutions Spectrophotometry, Infrared structure Xenopus Xenopus laevis Xenopus Proteins
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