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A shotgun proteomic method for the identification of membrane-embedded proteins and peptides.


ABSTRACT: 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.

SUBMITTER: Blackler AR 

PROVIDER: S-EPMC2765231 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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A shotgun proteomic method for the identification of membrane-embedded proteins and peptides.

Blackler Adele R AR   Speers Anna E AE   Ladinsky Mark S MS   Wu Christine C CC  

Journal of proteome research 20080607 7


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. ...[more]

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