Structural characterization of synthetic model peptides of the DNA-binding cI434 repressor by electrospray ionization and fast atom bombardment mass spectrometry.
The structural characterization of two synthetic model peptides of the cI434 repressor is described. Unequivocal determination of the structure was achieved by means of electrospray ionization mass spectrometry of the intact peptides and 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 characterizing synthetic peptides of relatively high molecular weight.
International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
P
P
Percipalle
R
R
Saletti
S
S
Pongor
S
S
Foti
A
A
Tossi
S
S
Fisichella
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D004268:DNA-Binding Proteins / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry*; D016339:Spectrometry, Mass, Fast Atom Bombardment; D014357:Trypsin; D014764:Viral Proteins
C063367:434-repressor protein, Bacteriophage 434; D004268:DNA-Binding Proteins; D010455:Peptides; D012097:Repressor Proteins; D014764:Viral Proteins; D002918:Chymotrypsin; D014357:Trypsin