title: Mass spectrometry for proteomics-based investigation.
abstract: Within the past years, we have witnessed a great improvement in mass spectrometry (MS) and proteomics approaches in terms of instrumentation, protein fractionation, and bioinformatics. With the current technology, protein identification alone is no longer sufficient. Both scientists and clinicians want not only to identify proteins but also to identify the protein's posttranslational modifications (PTMs), protein isoforms, protein truncation, protein-protein interaction (PPI), and protein quantitation. Here, we describe the principle of MS and proteomics and strategies to identify proteins, protein's PTMs, protein isoforms, protein truncation, PPIs, and protein quantitation. We also discuss the strengths and weaknesses within this field. Finally, in our concluding remarks we assess the role of mass spectrometry and proteomics in scientific and clinical settings in the near future. This chapter provides an introduction and overview for subsequent chapters that will discuss specific MS proteomic methodologies and their application to specific medical conditions. Other chapters will also touch upon areas that expand beyond proteomics, such as lipidomics and metabolomics.
authors: Biochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY, 13699-5810, USA.
authors: Alisa G
authors: AG
authors: Woods
authors: Izabela
authors: I
authors: Sokolowska
authors: Armand G
authors: AG
authors: Ngounou Wetie
authors: Kelly
authors: K
authors: Wormwood
authors: Roshanak
authors: R
authors: Aslebagh
authors: Sapan
authors: S
authors: Patel
authors: Costel C
authors: CC
authors: Darie
mesh_terms: D013058:Mass Spectrometry / Q000379:methods*; D020033:Protein Isoforms; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*
chemical_list: D020033:Protein Isoforms