Abstract
Publisher Summary This chapter discusses the principles and practical protocols involved in the mass spectrometric identification of yeast proteins. Mass spectrometry has improved the toolbox of biochemical strategies by providing rapid and high throughput identification of proteins in yeast. The wide variety of mass spectrometers available commercially can be distinguished by the way ions are produced (ion sources) and the way they are separated (mass analyzers). The most commonly used ion sources for biological applications are matrix-assisted laser desorption and ionization (MALDI) and electrospray (ES) ionization. Both of them are known as “soft ionization methods,” permitting the transfer of the biological compound into the gas phase of the mass analyzer without decomposition. A rapid and sensitive analysis of yeast protein complexes or interacting partners can be achieved by liquid chromatography–mass spectrometry (LC–MS) approaches. The combination of high-resolution mass spectrometry, data-dependent software, and nanoflow liquid chromatography allows the creation of a robust system for the characterization of complex mixtures. The chapter discusses the methods for protein identification.
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