Chromatographic benefits of elevated temperature for the proteomic analysis of membrane proteins.
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.
Blackler
Adele R
AR
Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Speers
Anna E
AE
Wu
Christine C
CC
D000818:Animals; D002853:Chromatography, Liquid / Q000295:instrumentation / Q000379:methods*; D008565:Membrane Proteins / Q000032:analysis*; D040901:Proteomics / Q000295:instrumentation / Q000379:methods*; D015203:Reproducibility of Results; D013696:Temperature
D008565:Membrane Proteins
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