| Literature DB >> 18537282 |
Adele R Blackler1, Anna E Speers, Mark S Ladinsky, Christine C Wu.
Abstract
Integral membrane proteins perform crucial cellular functions and are the targets for the majority of pharmaceutical agents. However, the hydrophobic nature of their membrane-embedded domains makes them difficult to work with. Here, we describe a shotgun proteomic method for the high-throughput analysis of the membrane-embedded transmembrane domains of integral membrane proteins which extends the depth of coverage of the membrane proteome.Mesh:
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Year: 2008 PMID: 18537282 PMCID: PMC2765231 DOI: 10.1021/pr700795f
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466