Abstract
The identification and characterization of herpes simplex virus protein interaction complexes are fundamental to understanding the molecular mechanisms governing the replication and pathogenesis of the virus. Recent advances in affinity-based methods, mass spectrometry configurations, and bioinformatics tools have greatly increased the quantity and quality of protein–protein interaction datasets. In this chapter, detailed and reliable methods that can easily be implemented are presented for the identification of protein–protein interactions using cryogenic cell lysis, affinity purification, trypsin digestion, and mass spectrometry.
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References
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Acknowledgements
I would like to thank Nathaniel Moorman for sharing his expertise in cryogenic lysis methods. I would also like to thank my mentors John Wills and Nancy Raab-Traub for providing excellent training environments where I acquired skills in affinity purification and mass spectrometry.
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Meckes, D.G. (2014). Affinity Purification Combined with Mass Spectrometry to Identify Herpes Simplex Virus Protein–Protein Interactions. In: Diefenbach, R., Fraefel, C. (eds) Herpes Simplex Virus. Methods in Molecular Biology, vol 1144. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-0428-0_14
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DOI: https://doi.org/10.1007/978-1-4939-0428-0_14
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