Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin: resonance assignments and secondary structure

A hybrid peptide of cecropin A and melittin was investigated by two-dimensional 1H-NMR at pH 5.8 in aqueous solution with 30% (by vol.) hexafluoroisopropanol. The peptide contains 26 amino acids, is a combination of the first 13 residues of each of the two parent peptides, CA(1-13)M(1-13) = CAM(1-26...

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Veröffentlicht in:	European journal of biochemistry 1991-07, Vol.199 (2), p.285-291
Hauptverfasser:	Sipos, D. (University of Stockholm, Sweden), Chandrasekhar, K, Arvidsson, K, Engstrom, A, Ehrenberg, A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Antimalarials Antimicrobial Cationic Peptides Biological and medical sciences cecropin A Fundamental and applied biological sciences. Psychology hybrids Hydrogen Insect Hormones - chemistry Insect Hormones - metabolism Magnetic Resonance Spectroscopy - methods Melitten - chemistry Melitten - metabolism melittin Molecular Sequence Data N.M.R PEPTIDE PEPTIDOS PROPIEDADES ANTIMICROBIANAS PROPRIETE ANTIMICROBIENNE Protein Conformation Protein Multimerization PROTEINAS PROTEINE Proteins Secondary structure
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