Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI

Piergiorgio Percipalle, Sandor Pongor, Sotir Zakhariev, Corrado Guarnaccia, Rosaria Saletti, Salvatore Foti, Salvatore Fisichella

Research output: Contribution to journalArticlepeer-review

Abstract

The synthesis and structural characterisation of the 1-63 N-terminal (Nter) sequence of the cI434 repressor is described. Matrix assisted laser desorption ionisation mass spectrometry of the intact peptide yielded a molecular weight determination of 6897.4, with respect to a calculated value of 6891.9. The correctness of the sequence was substantiated by fast atom bombardment mass spectrometric identification of complementary peptide fragments obtained by tryptic and chymotrypic digestion and partial separation by reversed-phase high-performance liquid chromatography. The results show the potential of this approach for characterising high molecular weight synthetic peptides.

Original languageEnglish (US)
Pages (from-to)151-159
Number of pages9
JournalEuropean Journal of Mass Spectrometry
Volume3
Issue number2
DOIs
StatePublished - 1997

Keywords

  • 434 repressor cI
  • DNA-binding proteins
  • Fast atom bombardment
  • Mass spectrometry
  • Matrix assisted laser desorption ionisation
  • Structural characterisation
  • Synthetic model peptides
  • Tryptic and chymotryptic cleavages

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Spectroscopy

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