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PROVIDES STRATEGIES AND CONCEPTS FOR UNDERSTANDING CHEMICAL PROTEOMICS, AND ANALYZING PROTEIN FUNCTIONS, MODIFICATIONS, AND INTERACTIONS--EMPHASIZING MASS SPECTROMETRY THROUGHOUT
Covering mass spectrometry for chemical proteomics, this book helps readers understand analytical strategies behind protein functions, their modifications and interactions, and applications in drug discovery. It provides a basic overview and presents concepts in chemical proteomics through three angles: Strategies, Technical Advances, and Applications. Chapters cover those many technical advances and applications in drug discovery, from target identification to validation and potential treatments.
The first section of Mass Spectrometry-Based Chemical Proteomics starts by reviewing basic methods and recent advances in mass spectrometry for proteomics, including shotgun proteomics, quantitative proteomics, and data analyses. The next section covers a variety of techniques and strategies coupling chemical probes to MS-based proteomics to provide functional insights into the proteome. In the last section, it focuses on using chemical strategies to study protein post-translational modifications and high-order structures.
Mass Spectrometry-Based Chemical Proteomics is an excellent source of information for readers in both academia and industry in a variety of fields, including pharmaceutical sciences, drug discovery, molecular biology, bioinformatics, and analytical sciences.
W. ANDY TAO, PHD, is a Professor in the Department of Biochemistry at Purdue University. He is also the Founder and Chief Scientific Officer at Tymora Analytical Operations, LLC, which provides lab R&D products for life sciences. Dr. Tao is the recipient of awards, such as the American Society of Mass Spectrometry Research Award, and author of more than 140 articles and book chapters on proteomics and mass spectrometry.
YING ZHANG, PHD, is a Professor at Fudan University. Her research focuses on the development of mass spectrometry-based new approaches for the analysis of low abundant proteins and posttranslational proteins.
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