A shotgun proteomic method for the identification of membrane-embedded proteins and peptides.
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.
Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
Adele R
AR
Blackler
Anna E
AE
Speers
Mark S
MS
Ladinsky
Christine C
CC
Wu
D002462:Cell Membrane / Q000737:chemistry; D019286:Endopeptidase K / Q000737:chemistry; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis* / Q000737:chemistry; D008854:Microscopy, Electron; D010455:Peptides / Q000032:analysis* / Q000737:chemistry; D040901:Proteomics / Q000379:methods; D053719:Tandem Mass Spectrometry
D008565:Membrane Proteins; D010455:Peptides; D019286:Endopeptidase K