Using stable isotope tagging and mass spectrometry to characterize protein complexes and to detect changes in their composition
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Author / Producer
Date
2007
Publication Type
Book Chapter
ETH Bibliography
yes
Citations
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Rights / License
Abstract
One of the primary goals of proteomics is the description of the composition, dynamics, and connections of the multiprotein modules that catalyze a wide range of biological functions in cells. Mass spectrometry (MS) has proven to be an extremely powerful tool for characterizing the composition of purified complexes. However, because MS is not a quantitative technique, the usefulness of the data is limited. For example, without quantitative measurements, it is difficult to detect dynamic changes in complex composition, and it can be difficult to distinguish bona fide complex components from nonspecifically copurifying proteins. In this chapter, we describe a strategy for characterizing the composition of protein complexes and their dynamic changes in composition by combining affinity purification approaches with stable isotope tagging and MS. The use of software tools for statistical analysis of the data is also described.
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Publication status
published
Editor
Book title
Quantitative Proteomics by Mass Spectrometry
Journal / series
Volume
359
Pages / Article No.
17 - 35
Publisher
Humana Press
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
Mass spectrometry; stable isotope tagging; ICAT reagents; quantification; protein complex; dynamics; affinity purification; SEQUEST; Peptide Prophet; Protein ASAPratio
Organisational unit
03663 - Aebersold, Rudolf (emeritus) / Aebersold, Rudolf (emeritus)