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.
Blackler
Adele R
AR
Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
Speers
Anna E
AE
Ladinsky
Mark S
MS
Wu
Christine C
CC
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