Abstract
With whole genomes being sequenced almost routinely, the next logical step towards a better understanding of cellular mechanisms lies in studying the functional units of gene expression - proteins. One of the fundamental approaches in proteomics is the use of two-dimensional gel electrophoresis as a mode of separation and visualization of complex protein mixtures. Despite several limitations of the method, its ability to separate large numbers of proteins, including their post-translationally modified forms, ensures that it will continue to be popular in several well-defined areas of proteomics. In this article, we discuss the merits and drawbacks of two-dimensional gels and compare them with alternative systems such as one-dimensional gels and liquid chromatography-based separation methods. In the wake of recent advances in mass spectrometry and related areas, we outline areas where two-dimensional gels can best be utilized as the preferred separation method in proteomic strategies.
Original language | English (US) |
---|---|
Pages (from-to) | 195-205 |
Number of pages | 11 |
Journal | Biomolecular Engineering |
Volume | 18 |
Issue number | 5 |
DOIs | |
State | Published - 2001 |
Keywords
- Cellular mechanisms
- Gel electrophoresis
- Proteomics
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Molecular Biology