A strategy for direct identification of protein S-nitrosylation sites by quadrupole time-of-flight mass spectrometry.

ABSTRACT: S-nitrosylation of proteins serves an important role in regulating diverse cellular processes including signal transduction, DNA repair, and neurotransmission. Identification of S-nitrosylation sites is crucial for understanding the significance of this post-translational modification (PTM) in modulating the function of a protein. However, it is challenging to identify S-nitrosylation sites directly by mass spectrometric (MS) methods due to the labile nature of the S-NO bond. Here we describe a strategy for direct identification of protein S-nitrosylation sites in an electrospray ionization (ESI) quadrupole time-of-flight (QTOF) mass spectrometer without prior chemical derivatization of S-nitrosylated peptides. Both sample buffer composition and MS hardware parameters were carefully adjust

SUBMITTER: Wang Y 

PROVIDER: S-EPMC2577058 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature