title: Targeted quantitation of proteins by mass spectrometry.
abstract: Quantitative measurement of proteins is one of the most fundamental analytical tasks in a biochemistry laboratory, but widely used immunochemical methods often have limited specificity and high measurement variation. In this review, we discuss applications of multiple-reaction monitoring (MRM) mass spectrometry, which allows sensitive, precise quantitative analyses of peptides and the proteins from which they are derived. Systematic development of MRM assays is permitted by databases of peptide mass spectra and sequences, software tools for analysis design and data analysis, and rapid evolution of tandem mass spectrometer technology. Key advantages of MRM assays are the ability to target specific peptide sequences, including variants and modified forms, and the capacity for multiplexing that allows analysis of dozens to hundreds of peptides. Different quantitative standardization methods provide options that balance precision, sensitivity, and assay cost. Targeted protein quantitation by MRM and related mass spectrometry methods can advance biochemistry by transforming approaches to protein measurement.
authors.affiliation: Department of Biochemistry and Jim Ayers Institute for Precancer Detection and Diagnosis, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6350, United States. daniel.liebler@vanderbilt.edu
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Liebler
authors.forename: Lisa J
authors.initials: LJ
authors.lastname: Zimmerman
mesh_terms: D013058:Mass Spectrometry / Q000379:methods*; D010455:Peptides / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis*; D040901:Proteomics / Q000379:methods; D012015:Reference Standards; D012680:Sensitivity and Specificity; D012984:Software; D053719:Tandem Mass Spectrometry
chemical_list: D010455:Peptides; D011506:Proteins