Analysis of posttranslational modifications of proteins by tandem mass spectrometry <subtitle>Mass Spectrometry For Proteomics Analysis</subtitle>
Protein activity and turnover is tightly and dynamically regulated in living cells. Whereas the three-dimensional protein structure is predominantly determined by the amino acid sequence, posttranslational modification (PTM) of proteins modulates their molecular function and the spatial-temporal dis...
| Published in: | BioTechniques |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2006-06-01
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| Online Access: | https://www.future-science.com/doi/10.2144/000112201 |
| Summary: | Protein activity and turnover is tightly and dynamically regulated in living cells. Whereas the three-dimensional protein structure is predominantly determined by the amino acid sequence, posttranslational modification (PTM) of proteins modulates their molecular function and the spatial-temporal distribution in cells and tissues. Most PTMs can be detected by protein andpeptide analysis by mass spectrometry (MS), either as a mass increment or a mass deficit relative to the nascent unmodified protein. Tandem mass spectrometry (MS/MS) provides a series of analytical features that are highly useful for the characterization of modified proteins via amino acid sequencing and specific detection of posttranslationally modified amino acid residues. Large-scale, quantitative analysis of proteins by MS/MS is beginning to reveal novel patterns and functions of PTMs in cellular signaling networks and bio-molecular structures. |
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| ISSN: | 0736-6205 1940-9818 |