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.
Synthesis and mass spectrometric characterisation of the N-terminal (1-63)DNA-binding domain of the bacteriophage 434 repressor cI
SALETTI, Rosaria;FOTI, Salvatore;
1997-01-01
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
