Seminar

How to make movies with mass spectrometry?

조회수 : 230 등록일 : 2015.10.08 09:59

일시 : 2015.10.07 17:00
소속 : GIST 기초과학부
발표자 : 김태영
장소 : R404
Mass spectrometry (MS) has become a standard platform for the analysis of biomolecules since the advent of matrix‐assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI). The structural information needed for the identification and characterization of biomolecules is obtained typically from tandem MS. Ultraviolet (UV) photodissociation (PD) deposits a well‐defined high energy into ions of interest in a very short timescale and results in tandem mass spectra that are dissimilar to those observed with other fragmentation methods. A hybrid linear ion trap/time‐of‐flight mass spectrometer with an ESI source was developed for UV PD of biomolecules, particularly peptide ions. This instrument enabled time‐dependent observations of product ions generated by 157 nm PD of peptide ions. Time resolved detection of UV PD fragment ions of phosphopeptides also made it possible to measure the timescale on which the phosphate group is lost from either precursor or product ions. Mass spectrometric measurement of biomolecular turnover is the second part of the presentation. To study biomolecular turnover, incorporation of a tracer into biomolecule is measured over a time. Heavy water (2H2O) has been employed as a tracer in turnover studies. The fractional synthesis rates of proteins and lipids have been measured using 2H2O labeling. The basic principles relevant to these studies and results are presented.
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