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Deep insights into the plant proteome by pretreatment with combinatorial hexapeptide ligand libraries.
J. Proteomics 74, 1182-1189 (2011)
Proteome analyses suffer from the large complexity of even small proteomes. Additionally, in many protein samples a few highly abundant proteins are hindering detailed proteomic studies, since they mask low abundant proteins. Recently, a new technology has emerged, which reduces dynamic range of protein concentrations within a given sample using combinatorial hexapeptide ligand libraries (CPLLs). This technique has been widely used in the microbial, animal and human fields and is now going to enter plant research. It can be a useful tool for fractionation of protein samples and might help to get a deeper insight into specific plant proteomes. In this review we describe the CPLL protein fractionation, summarize its possible applications in the plant field and discuss the limitations of this method.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Low abundant proteins; ProteoMiner; Sample fractionation; Combinatorial hexapeptide libraries; Dynamic range; Plant proteome
Language
Publication Year
2011
HGF-reported in Year
2011
ISSN (print) / ISBN
1874-3919
e-ISSN
1876-7737
Journal
Journal of Proteomics
Quellenangaben
Volume: 74,
Issue: 8,
Pages: 1182-1189
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Research Unit Environmental Simulation (EUS)
POF-Topic(s)
30202 - Environmental Health
Research field(s)
Environmental Sciences
PSP Element(s)
G-504900-002
PubMed ID
21354349
Scopus ID
79960978690
Erfassungsdatum
2011-09-15