Premium
Chromatographic benefits of elevated temperature for the proteomic analysis of membrane proteins
Author(s) -
Blackler Adele R.,
Speers Anna E.,
Wu Christine C.
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800210
Subject(s) - membrane protein , proteomics , computational biology , membrane , chemistry , integral membrane protein , chromatography , biology , biochemistry , gene
Integral membrane proteins (IMPs) perform crucial cellular functions and are the primary targets for most pharmaceutical agents. However, the hydrophobic nature of their membrane‐embedded domains and their intimate association with lipids make them difficult to handle. Numerous proteomic platforms that include LC separations have been reported for the high‐throughput profiling of complex protein samples. However, there are still many challenges to overcome for proteomic analyses of IMPs, especially as compared to their soluble counterparts. In particular, considerations for the technical challenges associated with chromatographic separations are just beginning to be investigated. Here, we review the benefits of using elevated temperatures during LC for the proteomic analysis of complex membrane protein samples.