Mass spectrometry global proteomics

Blonder J, Goshe MB, Xiao W, Camp DG, Wingerd M, Davis RW, Smith RD. Global analysis of the membrane subproteome of Pseudomonas aeruginosa using liquid chromatography-tandem mass spectrometry. J Proteome Res. 2004 3(3) 434 4. doi 10.1021/pr034074w. 

Global proteomic techniques are used for biological problems for which no molecular entry point is known. The idea is that changes in a cellular system can be understood better by analyzing its entire protein content quantitatively. The main analytical tools are a global and quantitative protein display and mass spectrometry to characterize the proteins that were identified for showing relevant quantitative changes. 

Cohen, A.M., Rumpel, K., Coombs, C.H. and Wastling, J.M. (2002) Characterisation of global protein expression by two-dimensional electrophoresis and mass spectrometry proteomics of Toxoplasma gondii. International Journal for Parasitology 32, 39-51. 

Radulovic D, Jelveh S, Ryu S, et al. Informatics platform for global proteomic profiling and biomarker discovery using liquid-chromatography-tandem mass spectrometry. Mol Cell Proteomics 2004 21 21. 

Fig. 4 Identification of alkyne-tagged P-lactone probes that target ClpP in S. aureus using click-chemistry, in-gel fluorescence and mass spectrometry. Subsequently, lead compounds were administered to 5. aureus and changes to the global bacterial proteome monitored. Particularly, changes to the levels of haemolysis and proteolysis enzymes (haemolysins, proteases, lipases and...

Global protein changes Proteomics approaches such as 2D gel electrophoresis, HPLC and mass spectrometry... 

Proteomics is often cited as the global (genome-wide) study of protein expression in a given living cell, tissue, or organism. Over the past decade, tandem mass spectrometry (MS/MS) has emerged as an essential analytical tool for large-scale... 

The biochemical approach of two-dimensional electrophoresis which has become the classical proteomic approach to whole proteome analysis has the capacity to display a large number of proteins expressed the studied system under given physiological conditions. Construction of global expression maps for defined proteomes is the most widely used application of proteomics and when used in combination with mass spectrometry (MS) techniques can be a powerful approach. There have been a number of studies focused on global neuroproteomics from whole brain analysis to the analysis of synaptic components. Two-dimensional maps have been constructed for whole human (Langen, Bemdt et al. 1999) mouse (Gauss, Kalkum et al. 

The most common proteomics approach uses two-dimensional gel electrophoresis to separate cellular proteins, followed by in-gel tryptic digestion of the protein spots and identification of the peptide sequences by mass spectrometry. There are s ificant problems with this approach, which so far, have limited its usefulness for drug taiget discovery. A number of protein classes such as int ral membrane proteins, positively chaiged and hydrophobic proteins are difficult to separate. There are often selective losses of individual protdns, for reasons that are not well understood, so the claim for a global picture is not entirefy accurate. The approach is semi-quantitative at best. Importantly, low abundance proteins may not be detected. However, newer approaches are constantly being developei Approaches which... 

Maass, S. et al (2011) Efficient, global-scale quantification of absolute protein amounts by integration of targeted mass spectrometry and two-dimensional gel-based proteomics. Anal Chem., 83 (7), 2677-2684. 

Molina, H. Horn, D.M. Tang, N. Mathivanan, S. Pandey, A. Global proteomic profiling of phosphopeptides using ETD tandem mass spectrometry. Pmc. Natl. Acad. Sci. 2007,104, 2199-2204. 

Hawkridge, A.M., Muddiman, D.C. mass spectrometry-based biomarker discovery toward a global proteome index of individuality. Ann. Rev. Anal. Chem. 2, 265-277 (2009)... 

---