PuSH - Publication Server of Helmholtz Zentrum München

Deep insights into the plant proteome by pretreatment with combinatorial hexapeptide ligand libraries.

J. Proteomics 74, 1182-1189 (2011)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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.
Altmetric
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Low abundant proteins; ProteoMiner; Sample fractionation; Combinatorial hexapeptide libraries; Dynamic range; Plant proteome
ISSN (print) / ISBN 1874-3919
e-ISSN 1876-7737
Quellenangaben Volume: 74, Issue: 8, Pages: 1182-1189 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed