Proteomics spectroscopy

Structural genomics is the systematic effort to gain a complete structural description of a defined set of molecules, ultimately for an organism s entire proteome. Structural genomics projects apply X-ray crystallography and NMR spectroscopy in a high-throughput manner. 

Griffin, T.J. and Abersold, R., Advances in proteomic analysis by mass spectroscopy, /. Biol. Chem., 276, 45497-45500, 2001. 

Figure 6 The SELDI technology. This type of proteomic analytical tool is a class of mass spectroscopy instrument that is useful in high-throughput proteomic fingerprinting of serum. Using a robotic sample dispenser, 1 p,L of serum is applied to the surface of a protein-binding chip. A subset of the proteins in the sample binds to the surface of the chip. The bound proteins are treated with a matrix-assisted laser desorption and ionization matrix and are washed and dried. The chip, which contains multiple patient samples, is inserted into a vacuum chamber where it is irradiated with a laser. The laser desorbs the adherent proteins and causes them to be launched as ions. The TOF of the ion before detection by an electrode is a measure of the mass-to-charge (m/z) value of the ion. The ion spectra can be analyzed by computer-assisted tools that classify a subset of the spectra by characteristic patterns of relative intensity (adapted from www.evmsdoctors.com).

Combining affinity chromatography, two-dimensional electrophoresis, and mass spectroscopy, Becamel and colleagues pioneered a global proteomic approach to 5-HT receptosomes (Chapter 7). These groundbreaking studies employed either the entire or partial carboxyl terminus of the 5-HT2 receptors as bait and heralded the discovery of multiple FRAPs (14,15). Since then, the proteomic strategy has been successfully applied to other 5-HT receptor subtypes (16,17). 

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