title: Identification and quantification of protein posttranslational modifications.
abstract: Posttranslational modifications (PTMs) of proteins perform crucial roles in regulating the biology of the cell. PTMs are enzymatic, covalent chemical modifications of proteins that typically occur after the translation of mRNAs. These modifications are relevant because they can potentially change a protein's physical or chemical properties, activity, localization, or stability. Some PTMs can be added and removed dynamically as a mechanism for reversibly controlling protein function and cell signaling. Extensive investigations have aimed to identify PTMs and characterize their biological functions. This chapter will discuss the existing and emerging techniques in the field of mass spectrometry and proteomics that are available to identify and quantify PTMs. We will focus on the most frequently studied modifications. In addition, we will include an overview of the available tools and technologies in tandem mass spectrometry instrumentation that affect the ability to identify specific PTMs.
authors.affiliation: Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee, USA.
authors.forename: Adam R
authors.initials: AR
authors.lastname: Farley
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Link
mesh_terms: D000818:Animals; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D008954:Models, Biological; D011499:Protein Processing, Post-Translational / Q000502:physiology; D011506:Proteins / Q000032:analysis* / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
chemical_list: D011506:Proteins