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Factors affecting the fast atom bombardment mass spectrometric analysis of proteolytic digests of proteins
Author(s) -
Pucci Pietro,
Sepe Ciro,
Marino Gennaro
Publication year - 1992
Publication title -
biological mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1052-9306
DOI - 10.1002/bms.1200210106
Subject(s) - chemistry , fast atom bombardment , peptide , proteolytic enzymes , mass spectrometry , amino acid , peptide sequence , bottom up proteomics , chromatography , mass spectrum , hydrogen bond , matrix (chemical analysis) , enzyme , molecular mass , protein mass spectrometry , biochemistry , molecule , tandem mass spectrometry , organic chemistry , gene
The fast atom bombardment (FAB) mass spectrometric analysis of proteolytic digests of proteins is currently used in protein structural characterization. The major current limitation of this procedure is that not all the peptides generated by enzyme digestion can be observed in the spectra. Previous studies showed that in a mixture the more hydrophilic peptides are suppressed. Several enzymatic digests of 18 different proteins ranging from 10 kDa to 67 kDa in molecular weight were examined using FAB mass spectrometry. It was observed that, even though the hydrophobicity of peptides is a factor in determining their presence or absence in the spectra, the predictions of whether or not a peptide would be detected based on this criterion varies in a wide range of values. Moreover, present results seem to indicate that the presence of particular amino acid side chains within a peptide sequence capable of forming hydrogen bonds with the matrix heavily affects the behaviour of that peptide in the mixture, despite the overall hydrophobicity of the peptide itself.