Traveling-wave ion mobility mass spectrometry analysis of isomeric modified peptides arising from chemical cross-linking
| Autor: | Eduardo Jorge Pilau, Fabio C. Gozzo, Alexandre F. Gomes, Amadeu H. Iglesias, Luiz Fernando Arruda Santos |
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| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
education.field_of_study Stereochemistry Ion-mobility spectrometry Protein Conformation Lysine Population Molecular Sequence Data Peptide Sequence (biology) Hydrogen-Ion Concentration Mass spectrometry Proteomics Spectral line Mass Spectrometry Ion Crystallography Cross-Linking Reagents chemistry Isomerism Structural Biology Amino Acid Sequence education Peptides Spectroscopy |
| Zdroj: | Journal of the American Society for Mass Spectrometry. 21(12) |
| ISSN: | 1879-1123 |
| Popis: | Traveling-wave ion mobility (TWIM) coupled to mass spectrometry (MS) has emerged as a powerful tool for structural and conformational analysis of proteins and peptides, allowing the analysis of isomeric peptides (or proteins) with the same sequence but modified at different residues. This work demonstrates the use of the novel TWIM-MS technique to separate isomeric peptide ions derived from chemical cross-linking experiments, which enables the acquisition of distinct product ion spectra for each isomer, clearly indicating modification on different sites. Experiments were performed with four synthetic peptides, for which variable degrees of mobility separation were achieved. In cases of partially overlapping mobility arrival time distributions (ATDs), extracting the ATDs of fragment ions belonging to each individual isomer allowed their separation into two distinct ATDs. Accumulation over regions from the specific ATDs generates the product ion spectrum of each isomer, or a spectrum highly enriched in their fragments. The population of both modified peptide isomers was correlated with the intrinsic reactivities of different Lys residues from reactions conducted at different pH conditions. |
| Databáze: | OpenAIRE |
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