Deep Imaging: How Much of the Proteome Does Current Top-Down Technology Already Resolve?

Publisher:
Public library of Science
Publication Type:
Journal Article
Citation:
PLoS One, 2014, 9 (1), pp. e86058 - e86058
Issue Date:
2014-01
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The main obstacle to effective and comprehensive proteome analysis has ostensibly been resolution. A variety of methods have been investigated in order to resolve ever smaller quantities of protein and detect them quantitatively [1–4]. One of the original and most powerful methods has been two-dimensional gel electrophoresis (2DE) [5]. Not only does this yield a position in a gel indicating isoelectric point (pI) and molecular weight, it does so with high reproducibility, and also resolves protein variants including isoforms and post-translationally modified forms (i.e. protein species [6]). While much dogma was associated with this method for a number of years, many of the suggested resolution issues have been addressed, enabling the full spectrum of proteins to be resolved by a refined, standardized protocol for sample preparation and 2DE [7–8]. This was largely achieved through the introduction of commercial immobilized pH gradient (IPG) strips [9–11], fine tuning of buffer, reducing and detergent components, and the use of fractionation to improve proteome coverage [8,12–13].
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