title: Affinity purification combined with mass spectrometry to identify herpes simplex virus protein-protein interactions.
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.
authors.affiliation: Department of Biomedical Sciences, College of Medicine, Florida State University, 115 W. Call Street, Tallahassee, FL, 32306-4300, USA, David.Meckes@med.fsu.edu.
authors.forename: David G
authors.initials: DG
authors.lastname: Meckes
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D008967:Molecular Biology / Q000379:methods*; D060066:Protein Interaction Maps / Q000235:genetics*; D040901:Proteomics / Q000379:methods; D018139:Simplexvirus / Q000235:genetics* / Q000378:metabolism; D053719:Tandem Mass Spectrometry / Q000379:methods; D014764:Viral Proteins / Q000096:biosynthesis*
chemical_list: D014764:Viral Proteins