Abstract
The first mass spectrometry device was made in 1912 by J. J. Thomson. Until the early 1900s, the analysis of small molecules was mainly performed using electronic ionization (EI) and chemical ionization (CI) methods. However, in 1969 Beckey and others developed the electric field desorption (FD) method to analyze the molecular weight distribution of high molecular weight compounds. In subsequent years, electrospray ionization (ESI) and the matrix-assisted laser desorption/ionization (MALDI) methods have been widely used for the analysis of high molecular weight compounds such as proteins and sugars. Significant progress has been made in genomic analysis. For the proteome to be analyzed (e.g., all proteins can be included in an individual sample), mass spectrometry is needed. Recently, mass spectrometry has played an important role in the analysis of protein complexes, particularly in determining the stoichiometry of protein within complexes as well as proteomic analysis. Importantly, the mass measurement of molecular complexes composed of proteins or of proteins and low molecular weight compounds through non-covalent interactions has been enabled, accelerating the understanding of biological phenomena and drug development. In this chapter, we describe the use of mass spectrometry for the analysis of non-covalent protein–protein interactions and protein–low molecular weight compound complexes. We also discuss the validation of the molecular masses of proteins within protein complexes by using mass spectrometry.
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Noda, M., Fukui, K., Uchiyama, S. (2016). Mass Spectrometry. In: Senda, T., Maenaka, K. (eds) Advanced Methods in Structural Biology. Springer Protocols Handbooks. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56030-2_11
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DOI: https://doi.org/10.1007/978-4-431-56030-2_11
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