4.5 Review

Chromatographic benefits of elevated temperature for the proteomic analysis of membrane proteins

Journal

PROTEOMICS
Volume 8, Issue 19, Pages 3956-3964

Publisher

WILEY
DOI: 10.1002/pmic.200800210

Keywords

Column heater; Liquid chromatography; Membrane proteins; Shotgun proteomics

Funding

  1. National Institutes of Health [DA022825, AA007464, AA016171, AA016653, DA021744]
  2. NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM [U01AA016653, R01AA016171, T32AA007464] Funding Source: NIH RePORTER
  3. NATIONAL INSTITUTE ON DRUG ABUSE [R21DA021744, F31DA022825] Funding Source: NIH RePORTER

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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.

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