Matrix-assisted laser desorption/ionization mass spectra reflect solution-phase zinc finger peptide complexation.
The complexation between an 18-residue zinc finger peptide of CCHC type (CCHC = Cys-X2-Cys-X4-His-X4-Cys, X = variable amino acid) from the gag protein p55 of human immunodeficiency virus type 1 (HIV-1) and various transition metal ions was studied by means of circular dichroism spectroscopy and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). A correlation between the complexation behavior in solution and in MALDI-MS could be established. It was shown that MALDI-MS is a fast method suitable for studying metal binding properties of zinc finger complexes.
Lehmann
E
E
Laboratory of Organic Chemistry, ETH Zürich, Switzerland.
Zenobi
R
R
Vetter
S
S
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D015683:Gene Products, gag / Q000737:chemistry; D015497:HIV-1 / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D011498:Protein Precursors / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D016335:Zinc Fingers
D015683:Gene Products, gag; D010455:Peptides; D011498:Protein Precursors; C059767:p55 gag precursor protein, Human immunodeficiency virus 1