A researcher s guide to mass spectrometry-based proteomics
#MMPMID27553853
Savaryn JP
; Toby TK
; Kelleher NL
Proteomics
2016[Sep]; 16
(18
): 2435-43
PMID27553853
show ga
Mass spectrometry (MS) is widely recognized as a powerful analytical tool for
molecular research. MS is used by researchers around the globe to identify,
quantify, and characterize biomolecules like proteins from any number of
biological conditions or sample types. As instrumentation has advanced, and with
the coupling of liquid chromatography (LC) for high-throughput LC-MS/MS, a
proteomics experiment measuring hundreds to thousands of proteins/protein groups
is now commonplace. While expert practitioners who best understand the operation
of LC-MS systems tend to have strong backgrounds in physics and engineering,
consumers of proteomics data and technology are not exposed to the
physio-chemical principles underlying the information they seek. Since articles
and reviews tend not to focus on bridging this divide, our goal here is to span
this gap and translate MS ion physics into language intuitive to the general
reader active in basic or applied biomedical research. Here, we visually describe
what happens to ions as they enter and move around inside a mass spectrometer. We
describe basic MS principles, including electric current, ion optics, ion traps,
quadrupole mass filters, and Orbitrap FT-analyzers.
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