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Eur. J. Mass Spectrom. 3, 151 - 159 (1997)

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 and Corrado Guarnaccia
International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy.
Rosaria Saletti, Salvatore Foti* and Salvatore Fisichella
Dipartimento di Scienze Chimiche, Università di Catania, Viale A.Doria, 6, I-95125 Catania, Italy.

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.

Keywords: 434 Repressor cI, DNA-binding proteins, synthetic model peptides, structural characterisation, matrix assisted laser desorption ionisation, fast atom bombardment, mass spectrometry, tryptic and chymotryptic cleavages, reversed-phase high-performance liquid chromatography.

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