Protein chemistry, mass

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. 

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 provides a wealth of information for proteomics research, enzymology, and protein chemistry in general. The techniques require only miniscule amounts of sample, so they can be readily applied to the small amounts of protein that can be extracted from a two-dimensional electrophoretic gel. The accurately measured molecular mass of a protein is one of the critical parameters in its identification. Once the mass of a protein is accurately known, mass spectrometry is a convenient and accurate method for detecting changes in mass due to the presence of bound cofactors, bound metal ions, covalent modifications, and so on. 

K. Biemann, The Massachusetts Institute of Technology mass spectrometry school, Journal of the American Society for Mass Spectrometry 5 (1994) 332-338 K. Biemann, The coming of age of mass spectrometry in peptide and protein chemistry, Protein Science 4 (1995) 1920-1927. 

Matrix-assisted laser desorption-ionization ionizes molecules with molecular masses of 100-1,000,000 Da for analysis by MS and provides high sensitivity, high throughput, and simplicity of operation. MALDI combined with enzymatic reactions and protein chemistry can provide very useful information on molecular masses, peptide maps, and primary structure.15 MALDI-TOF MS can quickly and accurately determine unfractionated mixtures at concentrations below 100 fmol per liter. The obtained data are then calibrated with internal standards, monoisotopic masses are assigned for all prominent peaks, and the peptide list thus generated is used to identify the protein by using a suitable database.16... 

Amine oxidases are homodimers with subunit molecular masses generally in the range 70kDa to 95kDa with one copper ion and one organic cofactor per subunit. Eukaryotic amine oxidases are glycoproteins with carbohydrate contents estimated at 3nl0%. Further information on the protein chemistry of amine oxidase can be found in Knowles Yadav (1984) and Pettersson (1985). 

D. B. Kassel,T. G. Consler, M. Shallaby, P. Sekhri, N. Gordon, and T. Nadler, Direct coupling of an automated 2-dimensional microcolumn affinity chromatography-capillary HPLC system with mass spectrometry for biomolecule analysis. Techniques in Protein Chemistry VI, Academic Press, New York, 1995, pp. 39-46. 

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. 

Hyperlinks to other mass spectrometry, protein chemistry, or molecular biology sites. 

CipoUa, D.C. Shire, S.J. Analysis of oxidized human relaxin by reverse phase HPLC, mass spectrometry, and bioassays. In Techniques in Protein Chemistry II Academic Press New York, NY, 1991 543-555. 

Gradually, over the past twenty years, mass spectrometers were interfaced with a number of protein chemistry assays to generate detectors providing superior information. With the increased performance and versatility of the instrumentation dedicated to the life sciences, new analytical strategies for peptide and protein identification and characterization have emerged in which MS and bioinformatic tools are key players. MS has an enormous impact on the capability for structural analysis of bio-molecules, thanks to the ability to create gas phase ions of the peptides and proteins to be analyzed. Peptides and proteins are often charged and polar, making... 

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. 

ASQUITH, T.N., KEOUGH, T.W., GAUGGEL, D.L., TAKIGIKU, R SARLO, K. LACEY, M.P. (1994) Characterization by mass spectroscopy of conjugates between proteins and low molecular weight chemicals, in CRABB, J.W. (Ed.) Techniques in Protein Chemistry V PP- 11-18. New York Academic Press. 

The coupling of microfabricated devices to mass spectrometers has been a great success through the efforts of many laboratories around the world. The depth of applications has been limited by our ability to perform protein chemistry and biochemistry on a scale compatible with microfluidic devices. To date, microfluidic devices have been generally used to handle small amounts of sample. The next frontier for this field of research will be the development and integration of in situ chemical and biochemical processing. 

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... 

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