【摘 要】
:
Post-translational modifications (PTMs) of proteins play key roles in regulation of various biological functions of protein.Due to the dynamic complexities
【机 构】
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EwhaWomansUniversityKorea
【出 处】
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2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
Post-translational modifications (PTMs) of proteins play key roles in regulation of various biological functions of protein.Due to the dynamic complexities in vivo and low abundance of PTMs,however,comprehensive identification of PTMs remains a highly challenging problem in proteomics.Using existing approach,limited PTMs were identified by combining affinity-based enrichment and mass spectrometry analysis handling a few types of PTMs.We describe a new PTM-specific strategy,a selectively excluded mass screening analysis (SEMSA) of unmodified peptides in LC-ESI-q-TOF MS/MS in replicated runs of a purified protein on 2-dimensional gel.
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