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Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.

ABSTRACT: Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development.

SUBMITTER: Broncel M 

PROVIDER: S-EPMC4471546 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

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Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.

Broncel Malgorzata M   Serwa Remigiusz A RA   Ciepla Paulina P   Krause Eberhard E   Dallman Margaret J MJ   Magee Anthony I AI   Tate Edward W EW  

Angewandte Chemie (International ed. in English) 20150325 20

Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development. ...[more]