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Affinity purification combined with mass spectrometry to identify herpes simplex virus protein-protein interactions.

作者信息

Meckes David G

机构信息

Department of Biomedical Sciences, College of Medicine, Florida State University, 115 W. Call Street, Tallahassee, FL, 32306-4300, USA,

出版信息

Methods Mol Biol. 2014;1144:209-22. doi: 10.1007/978-1-4939-0428-0_14.

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.

摘要

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