Matrix-assisted laser desorption/ionization mass spectra reflect solution-phase zinc finger peptide complexation

J Am Soc Mass Spectrom. 1999 Jan;10(1):27-34. doi: 10.1016/S1044-0305(98)00116-0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Gene Products, gag / chemistry
  • HIV-1 / chemistry
  • Humans
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Protein Precursors / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Zinc Fingers*

Substances

  • Gene Products, gag
  • Peptides
  • Protein Precursors
  • p55 gag precursor protein, Human immunodeficiency virus 1