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Imaging Techniques in Proteomics Research

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Part of the book series: Translational Bioinformatics ((TRBIO,volume 6))

Abstract

Imaging has been used for several decades for the visual representation of cellular and molecular processes of living organisms in a two or three dimensional fashion. Several imaging techniques like X-rays, immunohistochemistry, nuclear magnetic resonance, cryo-electron microscopes, positron emission tomography, green fluorescent protein labelling etc., have been developed and used to understand the structure and function of biological compounds (Saito et al. 2012). These techniques have aided in study of the structure and function of several proteins thereby facilitating the understanding of various human diseases. As advancement to the available imaging methods, a new technique called the Mass Spectrometry Imaging (MSI) or the Imaging Mass Spectrometry (IMS) has gained momentum in the recent past and has enabled the analysis of spatial distribution of biomolecules like peptides, metabolites, proteins etc., as well as pharmaceutical compounds based on their molecular masses. In this chapter we focus on the various strategies used in MSI experiments, the types of compounds analysed and the methodology and analyses used by MSI.

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Acknowledgements

We would like to thank Nissi Anthony and Siva Raman PN for helping in manuscript preparation.

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Correspondence to Goutham Edula .

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Subramaniyam, D., Edula, G. (2014). Imaging Techniques in Proteomics Research. In: Marko-Varga, G. (eds) Genomics and Proteomics for Clinical Discovery and Development. Translational Bioinformatics, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9202-8_13

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