Mass based proteomics

Nelson, R. W., Nedelkov, D., and Tubbs, K. A. (2000). Biosensor chip mass spectrometry A chip-based proteomics approach. Electrophoresis 21, 1155-1163. 

Aebersold, R. Mann, M. Mass spectrometry-based proteomics. Nature 2003, 422, 198-207. 

Aebersold, R., Mann, M. (2003). Mass spectrometry-based proteomics. Nature 422,198-207. Alpert, A.J., Andrews, P.C. (1988). Cation-exchange chromatography of peptides on poly(2-sulfoethyl aspartamide)-silica. J. Chromatogr. 443, 85-96. 

Ong S, Mann M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 2005 1 252-262. 

Guerrero C, Tagwerker C, Kaiser P, et al. An integrated mass spectrometry-based proteomic approach quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol. Cell. Proteomics. 2006 5 366-378. 

General Strategy for Mass Spectrometry-Based Proteomics... 

MS instruments measure the mass-to-charge ratio (m/z) values of the smallest of molecules very accurately. In addition, the development of translated genomic databases and specialized software algorithms that rapidly search MS data against theoretical spectra of known or predicted proteins within databases is an important component that greatly facilitated the emergence of mass spectrometry-based proteomics as a key approach for large-scale proteomic analysis.15... 

FIGURE 15.1 Overview of configuration of MS and MS-based proteomic analysis. Proteins are extracted from biologic samples and fractionated by a variety of separation methods including gel separation, HPLC, and capillary electrophoresis. The common ion sources and mass analyzers used are indicated. 

The mass spectrometric information should ideally be sufficient to answer two questions about each sample what does it contain and how much In order to answer these questions appropriately a researcher has to face the three central problems of mass spectrometry based proteomic research (i) the design of the experiment to allow for detection of proteins that are present in low abundance in the biological system... 

R. Aebersold and M. Mann. Mass Spectrometry-Based Proteomics. Nature, 422(2003) 198-207. 

Reinders, J., Lewandrowski, U., Moebius, J. et al. (2004) Challenges in mass spectrometry-based proteomics. Proteomics, 4, 3686-703. 

Warnock, D.E., Fahy, E. and Taylor, S.W. (2004) Identification of protein associations in organelles, using mass spectrometry-based proteomics. Mass Spectrom. Rev., 23,259-80. 

MALDI and ESI represent the predominant ionization techniques in mass spectrometry-based proteomics, as recognized by the Nobel Prize in chemistry in 2002. MALDI is mainly used to volatize and ionize simple polypeptide samples for mass spectrometric (MS) analysis at high speed. The analysis of more complex peptide mixtures is usually conducted via ESI mass spectrometry (ESI MS) coupled online with a high-pressure liquid chromatography (HPLC) system to concentrate and separate peptides prior to MS analysis. 

Ohara, O., Mann, M., Jensen, O. N., Pandey, a. (2002). A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-spedfic antibodies identification of a novel protein, Frigg, as a protein kinase A substrate. Mol. Cell Proteomics 1, 517-527. 

Binz PA, Hochstrasser DF, Appel RD. Mass spectrometry-based proteomics current status and potential use in clinical chemistry. Clin Chem Lab Med 2003 41 1540-51. 

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