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Titolo:
THE IDENTIFICATION OF PEPTIDE MODIFICATIONS DERIVED FROM GEL-SEPARATED PROTEINS USING ELECTROSPRAY TRIPLE QUADRUPOLE AND ION-TRAP ANALYSES
Autore:
SWIDEREK KM; DAVIS MT; LEE TD;
Indirizzi:
ZYMOGENET INC,1201 EASTLAKE AVE E SEATTLE WA 98102 CITY HOPE NATL MED CTR,BECKMAN RES INST DUARTE CA 91010
Titolo Testata:
Electrophoresis
fascicolo: 6, volume: 19, anno: 1998,
pagine: 989 - 997
SICI:
0173-0835(1998)19:6<989:TIOPMD>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANDEM MASS-SPECTROMETRY; SEQUENCE DATABASES; POLIOVIRUS RNA; FRAGMENTS; MIXTURES; REGION; IV;
Keywords:
MICROELECTROSPRAY; ION TRAP MASS SPECTROMETRY; PEPTIDE MODIFICATIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
K.M. Swiderek et al., "THE IDENTIFICATION OF PEPTIDE MODIFICATIONS DERIVED FROM GEL-SEPARATED PROTEINS USING ELECTROSPRAY TRIPLE QUADRUPOLE AND ION-TRAP ANALYSES", Electrophoresis, 19(6), 1998, pp. 989-997

Abstract

Microspray tandem mass spectrometry (MS/MS) in combination with database search routines has become a powerful tool for the identification of proteins from femtomole amounts of material following gel electrophoresis and in-gel digestion procedures. However, artifactual modification of susceptible residues can arise during gel electrophoresis, leading to unexpected peptide mass shifts during mass analysis, Consequently, collision-induced dissociation (CID) spectra generated from these derivatized peptides can defy direct interpretation by automated database search routines and remain unidentified. Here, we evaluate the MS/MS spectra of peptides carrying oxidized derivatives of tryptophane and methionine residues, and various modifications of cysteine. We demonstrate that certain of these modifications generate characteristic fragmentation patterns or ''fingerprints'', during CID analysis, the knowledge of which can facilitate the interpretation of the spectra. We will show that these signature fragment ions are predominantly produced during the CID analysis of singly charged ions although they can be observed in the MS/MS spectra of the doubly charged species as well. In other cases, the CID spectrum lacks a characteristic fingerprint and the modification remains silent. However, CID spectra of related peptides, differing only by their modifications, are similar and all or partof the fragment ion spectra will have shifted by a discreet mass, which facilitates the identification of the modified residue. At the sametime, the comparison of related spectra can prevent misinterpretations such as the assignment of a residue mass to the wrong amino acid or a neutral loss fragment ion to a y- or b-ion.

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Documento generato il 24/10/20 alle ore 10:58:05