Protein chemistry mass spectrometry

M.E. Bier, Analysis of proteins by mass spectrometry. In G.C. Howard and W.E. Brown (Eds.), Modern Protein Chemistry, CRC Press, Boca Raton, 2002, pp. 71-102. 

Mass spectrometry has been an established analytical technique in organic chemistry for many years. Until recently, however, the very low volatility of proteins made mass spectrometry useless for the investigation of these molecules. 

Amino-acids, Peptides, and Proteins Carbohydrate Chemistry Catalysis Colloid Science Electrochemistry Electron Spin Resonance Environmental Chemistry General and Synthetic Methods Heterocyclic Chemistry Macromolecular Chemistry Mass Spectrometry Nuclear Magnetic Resonance Organometallic Chemistry Organophosphorus Chemistry Photochemistry... 

Mass spectrometry is now used to measure the mass of virtually any atom or molecule. In 2002, the Nobel Prize in chemistry was awarded for the study of proteins by mass spectrometry. 

Mass spectrometry has been an established analytical technique in organic chemistry for many years. Until recently, however, the very low volatility of proteins made mass spectrometry useless for the investigation of these molecules. This difficulty has been circumvented by the introduction of techniques for effectively dispersing proteins and other macromolecules into the gas phase. These methods are called matrix-assisted laser desorption-ionization (MALDI) and electrospray spectrometry. We will focus on... 

Miyagi, M., Nakazawa, T. (2008) Determination of pK values of individual histidine residues in proteins using mass spectrometry. Analytical Chemistry, 80 (17), 6481-6487. 

Bier, M. E. In Brown, W. E. Howard, G. C. (Eds.), Analysis of Proteins by Mass Spectrometry. Modern Protein Chemistry Practical Aspects, Catalog Number 9453 CRC Press, Boca Raton, FL 2002, pp. 71-101. 

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... 

Methods based on liquid chromatography-mass spectrometry (LC-MS) and universally accepted search algorithms permit reliable identifications of low levels of proteins at high sensitivity [6]. Even semispecialized protein chemistry labs can readily identify proteins at the level of a few picomoles (10 pmol of a 50-kDa protein is 500 ng). Specialized groups with access to the latest advances in HPLC and mass spectrometry routinely work with subpicomolar quantities. Chemical proteomics as discussed here requires the more advanced equipment. 

Koing, S. 2005. Functional protein analysis using mass spectrometry. Current Organic Chemistry 9(9), 875-887. Osguthorpe, D. 2000. Ab initio protein folding. Current Opinion in Structural Biology 10(2), 146-152. 

Moore, R. E., Licklider, L., Schumann, D., and Lee, T. D., A microscale electrospray interface incorporating a monolithic, poly(styrene-divinylbenzene) support for on-line liquid chromatography tandem mass spectrometry analysis of peptides and proteins. Analytical Chemistry 70(23), 4879-4884, 1998. 

Eigeys, D. and Aebersold, R., Nanoflow solvent gradient delivery from a microfabricated device for protein identifications by electrospray ionization mass spectrometry. Analytical Chemistry 70(18), 3721-3727, 1998. 

Powell, M. J., Sutton, J. N., Del Castillo, C. E., and Timperman, A. I., Marine proteomics Generation of sequence tags for dissolved proteins in seawater using tandem mass spectrometry. Marine Chemistry 95(3 ), 183-198, 2005. 

Kwon, S. W., Profiling of soluble proteins in wine by nano-high-performance liquid chromatography/ tandem mass spectrometry. Journal of Agricultural and Food Chemistry 52(24), 7258-7263, 2004. 

Recent developments in instrument design have led to lower limits of detection, while new ion activation techniques and improved understanding of gas-phase ion chemistry have enhanced the capabilities of tandem mass spectrometry for peptide and protein structure elucidation. Future developments must address the understanding of protein-protein interactions and the characterization of the dynamic proteome (Chalmers and Gaskell 2000). 

Griffiths, W.J. (2000). Nanospray mass spectrometry in protein and peptide chemistry. EXS, 88, 69-79. 

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