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 journalArticle

    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
    StatePublished - Dec 1 1997

    Fingerprint

    bacteriophages
    Bacteriophages
    peptides
    deoxyribonucleic acid
    Molecular weight
    Peptides
    Peptide Fragments
    molecular weight
    DNA
    High performance liquid chromatography
    synthesis
    Ionization
    Mass spectrometry
    Desorption
    liquid chromatography
    Atoms
    Lasers
    bombardment
    mass spectroscopy
    desorption

    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

    Cite this

    Percipalle, P., Pongor, S., Zakhariev, S., Guarnaccia, C., Saletti, R., Foti, S., & Fisichella, S. (1997). Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI. European Journal of Mass Spectrometry, 3(2), 151-159.

    Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI. / Percipalle, Piergiorgio; Pongor, Sandor; Zakhariev, Sotir; Guarnaccia, Corrado; Saletti, Rosaria; Foti, Salvatore; Fisichella, Salvatore.

    In: European Journal of Mass Spectrometry, Vol. 3, No. 2, 01.12.1997, p. 151-159.

    Research output: Contribution to journalArticle

    Percipalle, P, Pongor, S, Zakhariev, S, Guarnaccia, C, Saletti, R, Foti, S & Fisichella, S 1997, 'Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI', European Journal of Mass Spectrometry, vol. 3, no. 2, pp. 151-159.
    Percipalle, Piergiorgio ; Pongor, Sandor ; Zakhariev, Sotir ; Guarnaccia, Corrado ; Saletti, Rosaria ; Foti, Salvatore ; Fisichella, Salvatore. / Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI. In: European Journal of Mass Spectrometry. 1997 ; Vol. 3, No. 2. pp. 151-159.
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    AU - Zakhariev, Sotir

    AU - Guarnaccia, Corrado

    AU - Saletti, Rosaria

    AU - Foti, Salvatore

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