Meckes David G
Department of Biomedical Sciences, College of Medicine, Florida State University, 115 W. Call Street, Tallahassee, FL, 32306-4300, USA,
Methods Mol Biol. 2014;1144:209-22. doi: 10.1007/978-1-4939-0428-0_14.
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.
