Analysis of posttranslational modifications of proteins by tandem mass spectrometry: Mass Spectrometry For Proteomics Analysis. (June 2006)

• Record Type: Journal Article
• Authors: Larsen, Martin R.; Trelle, Morten B.; Thingholm, Tine E.; Jensen, Ole N.
• Is Part Of: Biotechniques. Volume 40:Number 6(2006)
• Page Start: 790
• Page End: 798
• Publication Date: 2006-06
• Subjects: Biology, Experimental -- Periodicals; Molecular biology -- Periodicals; Medical technology -- Periodicals; Biology, Experimental; Medical technology; Molecular biology; Clinical Laboratory Techniques -- Periodicals; Research -- Periodicals; Medical Laboratory Science -- Periodicals; Periodicals; Electronic journals; 570
• DOI: 10.2144/000112201
• Languages: English
• ISSNs: 0736-6205

Abstract

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.