|The identification and quantitative measurement of different forms of protein site-specific reversible cysteine modifications remain technically challenging. Many mass spectrometry (MS)-based workflows have been developed, all sharing a common principle of first blocking any free thiol before labeling the specific forms of cysteine modifications that can be reversed by specific reducing agents. In essence, this “switches” the reversibly modified cysteine into chemically labeled cysteine more suitable for MS-based detection and quantification. The recent availability of multiplexed iodoTMT, a set of isobaric mass tags that irreversibly label Cys-thiols, now facilitates determination of the relative degree of specific cysteine modifications under different redox conditions. In this webinar, Dr. Kay-Hooi Khoo (Academia Sinica, Taiwan) will describe how multiplexed iodoTMT has been used to sequentially and differentially tag S-nitrosylation and S-glutathionylation, allowing their dynamics to be delineatedDr. Khoo will answer questions from webinar attendees so be sure to attend and get answers from an expert!|
|Date & Time:|
|Sept 30, 2014 (Thursday) 23:00 (GMT+8)|
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