Characterization and quantitation of membrane proteomes using multidimensional MS-based proteomic technologies

Josip Blonder*, Thomas P. Conrads, Timothy D. Veenstra

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

37 Scopus citations

Abstract

A major goal of proteomics is to develop the methods that enable the systematic characterization of every protein within the cell or particular subcellular proteome using a single analytical platform. Although the equivalent has already been achieved in genomics, reaching this goal in proteomics represents a much greater challenge due to the wide dynamic range of protein expression, numerous post-translational modifications and remarkable physicochemical heterogeneity of proteins. A major analytical challenge has involved developing more effective means for proteome-scale investigations of membrane proteins, whose solubility differs drastically from that of cytoplasmic proteins. Fortunately, rapid progress has increased the ability to characterize this critically important class of proteins on a scale analogous to that of acqueous soluble proteins.

Original languageEnglish
Pages (from-to)153-163
Number of pages11
JournalExpert Review of Proteomics
Volume1
Issue number2
DOIs
StatePublished - 2004
Externally publishedYes

Keywords

  • Isotopic labeling
  • Mass spectrometry
  • Membrane proteomics
  • Multidimensional fractionation
  • Quantitation

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