Protein biological mass spectrometry

Electrospray in the mid 1980s revolutionized biological mass spectrometry, in particular in the field of protein and peptide sequence analysis. Electrospray is a concentration-dependent, rather than a mass-dependent process, and maximum sensitivity is achieved at low flow rates with high-concentration, low-volume samples (Griffiths 2000). Joint NMR, x-ray diffraction, electrophoresis, and chromatography techniques with mass spectrometry (MS) techniques would be a trend in the future. 

Biemann, K. (1990). Applications of tandem mass spectrometry to peptide and protein structure. In Burhngame, A.L., McCloskey, J.A., editors. Biological Mass Spectrometry. Elsevier, Amsterdam, 176. 

Chapman, J.R. (ed.) (2000) Methods in Molecular Biology, Mass Spectrometry of Proteins and Peptides, vol. 146, Humana Press, Totowa, NJ. 

A. P. Snyder, Interpreting Protein Mass Spectra, Oxford University Press, Oxford, UK, 2000. C. Dass. Principles and Practice of Biological Mass Spectrometry, Wiley-Interscience, New York, 2001. 

Includes structural biology, mass spectrometry, protein arrays, bioinformatics, high throughput screening (HTS) assays, protein chemistry, cell biology, signal transduction, and physiology, as related to functional and structural proteomics and methods papers. 

Knowledge about the subcellular localization of a protein may provide a hint as to the function of the protein. The combination of classic biochemical fractionation techniques for the enrichment of particular subcellular structures with the large-scale identification of proteins by mass spectrometry and bioinformatics provides a powerful strategy that interfaces cell biology and proteomics, and thus is termed subcellular proteomics. ... 

Michael Kinterand Nicholas E. Sherman Protein Sequencing and Identification Using Tandem Mass Spectrometry Chhabil Dass Principles and Practice of Biological Mass Spectrometry Mike S. Lee LC/MSApplications in Drug Development... 

Mann, M., Hojrup, R, and Roepstroff, R, Use of mass spectrometric molecular information to identify proteins in sequence databases. Biological Mass Spectrometry, 22, 338-345, 1993. 

Isotope dilution analysis for protein quantification with ICP-MS is usually performed by linked techniques based on the coupling to an effective separation method, such as HPLC or CE. Generally, proteins to be analyzed should contain ICP-MS-detectable elements, including both naturally occurring and artificially labeled. After introduction of the spike that has different isotopic composition from the analyte, the elemental isotope ratio can be measured in ICP-MS and thus the detectable elements can be absolutely quantified by use of the isotope dilution equation. If proteins have been identified with biological mass spectrometry, or the elemental stoichiometric ratios of proteins have been known, the amount of proteins can be deduced from the elemental concentration of the proteins. 

Table 5.5 Nomenclature of the ions formed in the mass spectral fragmentation of polypeptides. From Chapman, J. R. (Ed.), Protein and Peptide Analysis by Mass Spectrometry, Methods in Molecular Biology, Vol. 61, 1996. Reproduced by permission of Humana Press, Inc. 

J. R. (Ed.), Protein and Peptide Analysis by Mass Spectrometry, Methods in Molecular Biology, Vol. 61, 1996. 

Proteomics is an interdisciplinary science that includes biology, bioinformatics, and protein chemistry. The purpose of this book is to provide the reader with an overview of the types of questions being addressed in proteomics studies and the technologies used to address those questions. The first chapter is a concise outline of the field as it presently stands. The second chapter provides an overview of the use of 2D-gel electrophoresis and mass spectrometry to identify proteins, as well as post-translational... 

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