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A Ubiquitin-like System Mediates Protein Lipidation


Analysis of Post-Translational Modifications by Mass Spectrometry


Mass spectrometry (MS) represents a well-accepted and reliable method for the characterization of proteins. The method has great advantages in terms of throughput, accuracy, and sensitivity in measurements, which is well suited for the identification of a wide variety of proteins, such those separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE), and for the analysis of post-translational modifications of a protein, which play important roles in various biological events. Taking advantages of an accumulating protein sequence database, the former has been a routine task for overall profiling of proteins expressed in an organism or cell. The latter, especially, the analysis of unknown or multiple modifications is challenging and can be exhaustively achieved by tandem mass spectrometry (MS/MS) [1,2] (Fig. 1).


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